I obtained my bachelor's degree in solid-states physics, and my MSc in medical physics. My master's thesis was on surface plasmon resonance based biosensors with biological and medical applications. I joined Victor Acosta's lab to pursue my PhD degree in Optical Science and Engineering at University of New Mexico, working on nanophotonic magnetic resonance bio/chemical sensors using nitrogen vacancy centers in diamond.

‍

‍

My current research focuses on developing a new type of magnetic resonance sensor that uses laser interrogation of diamond to detect the type and behavior of complex molecules in their natural environment without altering the analyte. The Nuclear Magnetic Resonance (NMR) sensor uses a diamond chip in a picoliter (pL) solution. The NMR detection sensitivity depends on the number of nitrogen-vacancy (NV) centers that are located close enough to the diamond surface to sense external spins. Our motivation is to assist in monitoring drug delivery and early diagnosis of cancer.

‍

I am a young and zealous student. I was born and raised in Mumbai, India. I obtained a bachelors degree from Institute of Chemical Technology in Mumbai India. The atmosphere at the university was that of research, everyone from faculty to students wanted to contribute to the world through research. I was bitten by the research bug and applied to university across the world to get a Doctoral Position. As a second girl child from a lower middle class family, my parents, who never went to college, were apprehensive about this adventure I had dreamed up. I hope I have done them proud. I am excited to be a part of Dr. Robert Powers group at University of Nebraska Lincoln. I look forward to obtaining a postdoctoral position in the future and continue my academic journey.

My thesis research focuses on NMR-based metabolomics work to understand a few different biological systems. Along with some wonderful collaborators I have got the opportunity to work on understanding cellular communication in Pancreatic Cancer model, nitrogen metabolism in resistant Staphylococcus aureus to name a couple. Another aspect of my research work is to identify metabolite level biomarkers for early stage Multiple Sclerosis in different biofluids like urine and cerebrospinal fluid. This work has lead me to continue to develop paper-based devices for metabolite identification. All in all my work is targeted towards using NMR to better human disease management. Why I do what I do? I always had an intent to learn, to discover and analyze, more for the process of finding things out. The joy in finding things out is what keeps me going. NMR and metabolomics have been an interesting adventure for me so far. I am intrigued by NMR spectroscopy and see my self as a researcher in the field for a long time.

I am a PhD student in physics at Florida State University. As a graduate research assistant at National High Magnetic Lab, I work on magnetic resonance imaging and spectroscopy projects as well as MRI/NMR coil design and characterization. I am an international student and received my BS in physics from Tehran University in Iran. I really enjoy learning and working in the interdisciplinary area between physics, biomedical and RF engineering.

My PhD project is on magnetic resonance electrical property tomography (MREPT) at 21.1 T, which is the strongest pre-clinical MRI magnet in the world. In MREPT, electrical properties of the sample such as conductivity can be determined from electromagnetic interaction between the B1 field and the sample using convention MRI sequences. I have investigated the feasibility and error percentage of different conductivity mapping approaches at ultra-high field using phantoms with known conductivity values. I have been passionate about developing this technique because imaging tissue conductivity can be used as an additional diagnostic parameter, e.g. in tumor diagnosis. Improving the accuracy and precision of this technique can significantly increase its application in clinical studies.

I am currently a third year PhD student at the University of Toronto under the supervision of Prof. Andre Simpson. Outside of the lab, I would use up most of my resources travelling. Exploring the unknown feeds my curiosity. Also, I am a photographer wanna-be.

My research focuses on the development and application of comprehensive multiphase NMR. It allows for analyses of multiphase samples in their intact forms. It can differentiate components in difference phases and study the interaction on solid-liquid interface. It opens doors to better understanding of environmental processes and natural samples in a holistic way, without any perturbation to the samples.

After finishing undergraduate studies at the University of Belgrade in Serbia, I enrolled at the Weizmann Institute of Science as a PhD student with Marie Curie fellowship as a part of EUROPOL ITN project. Research in an international environment in Prof. Frydman's group has always been a big excitement and pleasure for me, always inspiring me to think outside the box.

Developing new NMR methods for sensitivity enhancement has always been one of the most important approach to boost the SNR. My research is based on utilizing CEST and DNP principles to improve the signal of low gamma nuclei and weak NOE and TOCSY cross peaks in multidimensional experiments as well as to allow detection of the signal in challenging experiments involving protein-ligand interactions. Smartly designing a pulse sequence and bringing multi-fold sensitivity enhancement to the NMR community, for free, is what I am aiming for.

I am a Ph.D. student in the group of Prof. Dr. Harald Schwalbe at the Goethe University in Frankfurt. During my studies, I got appealed to the NMR on biomolecules, while doing my internship at his group. My research focused on analysis of the conformational preferences of unstructured state of polypeptides. I characterized the influence of next-amino acid residue on the structural preferences in φ, ψ, χ1 conformational space. These investigations, in cooperation with Prof. Reinhard Schweitzer-Stenner from Drexel University, resulted in to two publications.My master thesis project involved NMR puls sequence programming and optimization of the conditions for successful experimental approach. The aim was to detect the fast exchangeable unpaired imino protons in RNA by using chemical exchange saturation transfer experiments (CEST). Conclusively it was shown that CEST NMR technique can be successfully implemented for detection of the fast exchangeable imino protons in dynamic and unpaired regions of RNA molecules as well as free nucleotides in solution. I am currently working on two research topics: 1) light dynamics of retinal disease relevant rhodopsin mutants and 2) rapid NMR and biophysical characterization of structure and dynamics of small proteins. Due to their size and difficulty in biochemical identification, small proteins encoded by small open reading frames have been overlooked in gene annotation in the earlier years. Nowadays, such proteins are being identified to play important roles in a broad range of cellular functions such as cell division, morphogenesis and stress response. The functional elucidation of these small proteins still remains a challenging task. To understand the molecular mechanism of action, the characterization of their structure and dynamics is of utmost importance. Therefore, I apply NMR as powerful technique to obtain the structures and dynamics of a number of small peptides in their apo state as well as in complexes with diverse cellular components.

Rhodopsin belongs to the largest GPCRs (Gprotein coupled receptor) membrane protein family in the human genome. Light absorption by rhodopsin is the initiation point for photoactivated signaling cascade in retinal rods. Point mutations in the protein sequence cause the defective signaling and lead to human night blindness diseases such as retinitis pigmentosa (PR) and congenital stationary night blindness (CSNB). In contrast to PR, where the majority of mutations are distributed over the whole sequence, only 4 single point mutations causing CSNB are located in the retinal binding pocket. Depending on the type of amino acid replaced against glycine attheG90position in the sequence, mutation can lead either to RP (G90V) or to CSNB (G90D).By light-triggered, time-resolved NMR in solution-state, in combination with flash photolysis experiments I investigate light-induced conformational changes and dynamics of the CSNB associated G90D rhodopsin mutant. In contrast to wt rhodopsin, the thermally stable wt and the G90D mutant do not precipitate upon illumination and remain stable even after incubation at RT for several hours. Furthermore, the introduced mutations lead to significant changes the kinetics of the photodecay of rhodopsin. The characterization of mutations at position 90 may thus provide important clues to understand the molecular basis of stationary and progressive retinal degeneration

I am a Phd student since two years at Chalmers University of Technology in the research group of Associate Professor Lars Nordstierna. My background is in applied physics with a MSc from Uppsala University.

Morphology of regenerated cellulose fibers is known to affect mechanical properties along with chemical accessibility and appearance. One essential part of the morphology description is to determine the molecular orientation distribution function of the cellulose chain segments, which are typically aligned in the fibers drawing direction. Using solid-state NMR spectroscopy and the intrinsic chemical shielding tensor properties, it is possible to probe molecular anisotropy and thereby the molecular orientation. The methodology is based on Rotor Synchronized Magic Angle Spinning, abbreviated ROSMAS, which was originally developed by Spiess and co-workers and conducted on polyethylene terephthalate along with other synthetic polymers. The data evaluation strongly depends on an accurate chemical shielding tensor description and therefore we have employed density functional theory (DFT) electronic structure calculations, using the gauge-independent atomic orbital method, to minimize the identified inconsistency in previously reported data.

I will be receiving my PhD in biochemistry at the end of this semester from The University of Akron. My long-term career goal is to become a structural biologist working for a major corporation developing new therapeutics for novel protein targets. I'm currently seeking a post doc to gain more experience working on elucidating new protein structures and am interested in further developing my NMR experience as well as learning cryo-EM.

I study protein-ligand interactions for drug discovery and material sciences using NMR and other methods. I'm interested in better understanding protein active site structures and how advances in this area will help us develop better therapeutics and create systems for developing more consistent precursor materials for manufacturing.

I am French-Canadian, but grew up in Syracuse, NY. I completed my undergraduate studies at SUNY University at Buffalo under the advisement of Dr. Thomas Szyperski. My research in Buffalo involved validating novel pulse sequences for large biomolecules. Currently, I am a graduate student at Yale University under the advisement of Dr. Patrick Loria. Personally, I enjoy playing soccer and ultimate with friends or reading fiction on my free time.

My research focuses on understanding the relationship between dynamic motions of enzymes and their catalysis. Specifically, determining how the rate of catalysis of protein tyrosine phosphatases is regulated by the motions of active site loops. I am also researching how modulation of loop motions changes the catalytic rate through mutants and post-translational modifications. I am passionate about my research because I believe in its impact to improve our knowledge of these enzymes and potentially the drug development targeting related diseases.

My name is David Guarin, I am a first year PhD student. I work in the "Laboratoir des Biomelecules" (LBM), at the Ecole Normal Superieur in Paris. My PhD is directed by Daniel Abergel and Dennis Kurzbach. I joined this laboratory one year ago for a Masters internship. I have bachelors degrees in fundamental physics and a masters degree in theoretical physics. NMR, is a highly experimental field that has many applications and presents so many challenges, puzzles to solve. In a subject as DNP my theoretical approach can be an asset to link the applications to the theory that is yet highly unknown. I am truly interested in what DNP has to offer to the understanding of the biology of the human being and the structure of the world itself.

Currently I am working on developing dissolution dynamic nuclear polarization (D-DNP) for the study of the "sleeping sickness". The idea is, for a short period of time enhancing the NMR signal of a substrate by at least 3 orders of magnitude. We then send it to a medium containing living cells or enzymes and we study the signal emitted by the substrate and the products. This study allows us to follow the kinetics of the chemical reactions due to the metabolism of the cells or the activity of the enzymes. Being able to study directly the cell metabolism and the enzyme activity is a very a powerful tool to understand the effect of different pathologies in the human body. At the same time I am working on a more theoretical subject. It consists of studying the nature of the DNP focusing on the Thermal Mixing, a method of polarization transfer of electrons to nuclei. We try to determine the context in which it takes place and the effects of this phenomena that transfers heat between different nuclei.

I was born and raised in Wooster, Ohio and received my B.S. from Ashland University. I started undergraduate research under Dr. Jeffrey Weidenhamer on natural products derived from Red Maple. I now work with Dr. Qi Zhang at UNC Chapel Hill, where I plan to graduate with a Ph.D. this year! I am an avid music fan and have been to over 100 concerts.

I work on small, cancer related RNAs using NMR. I'm passionate about my research because NMR is a powerful tool; I have revealed new and exciting things about RNA that would be impossible with other techniques. I am hopeful that my discoveries can be used to develop therapeutics in future work.

Rashik Ahmed received his Honors Bachelor’s degree in Biochemistry from McMaster University. For his senior thesis, he worked in the laboratory of Dr. Giuseppe Melacini on elucidating the molecular mechanism of the green tea extract EGCG as an Aβ oligomer remodeling agent. Since then, he has stayed on in the Melacini lab to pursue a PhD degree. His current research focuses on understanding the series of microscopic steps that lead to the formation of toxic oligomers, which underlie the pathogenesis of several neurodegenerative disorders.

Alzheimer’s disease (AD) is the leading cause of dementia worldwide and the incidence is expected to rise due to pervasive population ageing. AD imposes severe social and economic burdens and is estimated to cost over US $1 trillion worldwide. Substantial genetic, animal model and biochemical studies have suggested that the production, deposition and reduced clearance of toxic oligomers of the amyloid beta (Aβ) peptide play a central role in the etiology of the early phases of AD. Hence, a potential therapeutic strategy that has garnered attention in recent years is the development of Aβ aggregation inhibitors, either through small molecules or biologics, such as antibodies or plasma proteins. However, understanding the mechanism by which these inhibitors reduce oligomer toxicity and their translation to the clinical setting has been largely hindered due to the transient nature of the Aβ oligomer intermediates. To this end, my research capitalizes on recent advancements in solution NMR techniques that enable the detection of these short-lived intermediates, providing atomic-resolution structural insight. The mapping of these previously elusive structural features provide a foundation to establish structure-toxicity relationships of Aβ oligomers, and inform the design of new and more effective treatment strategies for AD.

I am a PhD student in Physics at Florida State University. As a graduate research assistant at National High Magnetic Lab, I work on projects related to magnetic resonance imaging and spectroscopy as well as MRI/NMR coil design and characterization. I have received my BS in Physics from Tehran University in Iran. I really enjoy working on the interdisciplinary area between physics, biomedical and RF engineering.

Replacing normal metal NMR coils with thin-film high-temperature superconducting (HTS) coils in cryogenically cooled NMR probes can significantly improve the sensitivity and signal-to-noise ratio (SNR) due to the high quality (Q) factor of superconducting resonators. The improved sensitivity is especially helpful for direct 13C detection due to its low gyromagnetic ratio and 1 % natural abundance. By using HTS coils in probes optimized for 13C detection, compounds with as little material as 40 nmols can be studied. However, the high Q factor will reduce the system bandwidth for both excitation and reception required for detection of 13C broad spectrum. To characterize and resolve these issues, I have studied the RF properties of an HTS thin film resonator designed to be used as a 13C NMR transceive coils in frequency and time domains.

I am 28 years old and a PhD student at the RWTH Aachen University in the B. Blümich group. As a part of the ACalNet " The Aachen-California Network of Academic Exchange " group, I also had the opportunity to carry out research and gain experience at the University of California, Berkeley in the group of J. Reimer.

In the last two decades, technical devices such as personal computers or mobile phones were miniaturized to profit from portability and simplified handling, while possessing enhanced functionality and performance. The same trend is observable for unilateral NMR sensors. Unfortunately, a miniaturization is often accompanied by losses in penetration depth and absolute signal quality and measurement time. My research deals with the hardware aspect of NMR sensor miniaturization and furthermore, different strategies of how these issues can be approached. Furthermore, my research concentrates on application of low-field NMR sensors in the fields of materials science and porous media. I utilize the profile NMR-MOUSE to characterize the stratigraphy, composition and possible molecular consequences of fabrication processes of different tires types. Another type of compact NMR sensors, the Halbach magnet, is employed to investigate Metal Organic Frameworks (MOFs) in terms of methane storage capability. Inverse Laplace Transform (ILT) is used to gain insights in the process of methane adsorption and desorption depending on pressure and temperature.

I am a PhD candidate at the University of California San Francisco researching hyperpolarized carbon-13 metabolic brain imaging. I earned my Master's Degree in 2015 studying Electrical Engineering from Stanford University while pursuing patent law for startups.

My research investigates the metabolism of hyperpolarized [2-13C]pyruvate through the TCA cycle and its conversion to [2-13C]lactate and [5-13C]glutamate in the human brain in volunteers. I am passionate about new and useful metrics that may elucidate methods for diagnosing and detecting early-stage neurodisorders.

I grew up in a small village in Germany and then moved to Frankfurt to study chemistry. Early during my studies, I got fascinated by NMR and joined the group of Prof. Harald Schwalbe. Today, I am a third year PhD student in his group. In my free time I enjoy travelling other countries, bouldering and reading.

My research focusses on the development of new heteronuclear-detected NMR experiments for the characterization of RNA. Here, heteronuclear-detected experiments often offer additional information when compared to proton-detected experiments, especially about flexible regions of RNA. This is especially valuable here as RNA is a very dynamic kind of biomolecule and therefore often difficult to characterize using conventional NMR experiments.

I am a phD student in Zhejiang University, I went to UC Berkeley as a visiting student in 2017 and spent 15 months here. I will graduate in this June and plan to pursue my academic career in Europe.

Solid-state NMR is a very powerful technique. I use this technology to study the structure and dynamics of the defects in Metal-organic frameworks. It can help us to see the microscopic world, the dancing of the molecules and the molecular interactions.

I received a B.S. in chemistry from the United States Naval Academy in 2008. After serving for six years and completing three deployments as a Surface Warfare Officer I transitioned out of the Navy, briefly working as a consultant before returning to graduate school at UC Irvine. My husband, Wyeth who is a graduate student in the Patterson lab at UCI, and I have a three-year-old rescue pug named Neptune. Outside of academics I enjoy doing game nights with friends, going on backpacking trips, almost anything to do with the ocean and dabbling in creative ventures. I am currently a Pedagogical Fellow at UCI and am excited to continue onto a career in academia.

My research project in the Martin Lab is on the design and construction of a triple-resonance switched-angle spinning (SAS) probe for the study and characterization of orientable media such as non-crystalline solids and membrane proteins. In the lab this will be used to study structures and aggregation pathways of eye-lens proteins that physiologically exist at very high concentrations as a hydrogel, and novel anti-microbials that we have identified from the carnivorous plant Drosera capensis. Recent focus has been on creating a generalizable approach to achieve optimized transceiver coil designs that will eventually be implemented into the SAS probe. This work has been accomplished by using multi-physics simulation software and 3D printing. In addition to my thesis work I have the opportunity to mentor undergraduate student researchers in several projects from characterization of carnivorous plant volatile organic compounds, to pigments that give rise to different colors in flowers. I am passionate about these interdisciplinary projects because I have had the opportunity to learn so much and grow as a scientist and mentor. I am grateful to be part of this community and to contribute to the future of NMR, which has a proud and extremely impactful history, while mentoring others in their own journey as scientists. To follow these projects check out our Instagram profile @martinlabuci!

I am a PhD student in the group of Prof. Blümich at the RWTH Aachen University in Germany and currently in my 2nd year. After finishing my B.Sc. at he most eastern part of germany - next to the border to Poland and the Czech Republik - I moved to the most western part of Germany - next to the border to the Netherlands and Belgium - for my M.Sc. in Polymer Sciences. After an internship in the very south of Germany I decided I wanted to further introduce modern low-field NMR techniques to industrial and polymer-relevant enviroments.In my free time I work on a voluntary basis for the local animal shelter and train some dogs until they find a new home.

My research is focusing on using benchtop NMR spectroscopy such that it will not only be seen as the highfield-NMRs' smaller brother, but rather as a powerful analytical tool for day-to-day labwork and also interesting scientific or industrial applications. For this I currently work on several projects. First we have designed and built a setup that allows to measure any proton or carbon containing gas or fluid pressurized up to 200 bar. This allows to easily access spectra and relaxation time of gases in a large pressure range and also opens the door to use benchtop NMR for high-pressure online reaction monitoring. Furthermore we investigate several oils in order to find out origins and nature of deposits which eventually will cause damage to the mechanical components that the oil is in contact with. I also designed another setup allowing the user to do photocatalytic reactions inside the magnet. Lastly we used compact NMR to identify and reliably quantify polymer additives. I enjoy my work a lot because I have large freedom of choice regarding my research. As I am always interested in learning new things and try to see the bigger picture this is much more appealing to me than having a set path to go. This way of working requires alot of self discipline, but I am able to try out alot of things that sometimes to not help me getting my PhD but at least satisfy my curiosity.

I am half-Irish and half-Polish, and completed my undergraduate studies in medicinal chemistry at Trinity College Dublin. I am now a second year PhD student in biochemistry at University College Dublin under the supervision of Dr. Chandralal Hewage where my research uses NMR and computational methods to study antimicrobial peptides. Last year, I helped in the organisation of the ICMRBS conference in Dublin. In my spare time, I enjoy reading fantasy, going on mountain walks, and travelling to new places.

My research focuses on using NMR and modelling techniques to model the structure of antimicrobial peptides and their interactions with their target biological membranes. The aim of my research is to further our understanding of how three-dimensional structure is related to the peptides’ biological activity. I use the NMR-derived structures in molecular dynamics simulations, which provide an atomistic insight into the peptides’ interactions. Additionally, I have a keen research interest in the intersection of peptide cheminformatics and machine learning.

I am a PhD candidate at the University of Nebraska-Lincoln. I received my undergraduate degree from a small liberal arts college, and after completing my PhD, I would like to return to a smaller, primarily undergraduate university as a professor. I would love to help others find a love for science as my mentors have done for me.

My research focuses on the protein Human DJ-1, which has been implicated in Parkinson's disease, emphysema and certain types of cancer. Importantly, a highly conserved cysteine residue, Cys106, may play a key role in disease progression, as over-oxidation of the residue causes a loss in structural integrity and increased dynamics of the protein. My work aims to characterize the structure and dynamics of the oxidative states of DJ-1, and their roles in diseases. As a scientist, it makes me excited to know that I have even just a small hand in furthering the understanding of devastating diseases such as Parkinson's disease.

My name is Kehinde Mary Taiwo. I am a second year Ph.D. and research student in the laboratory of Dr. Dayie Kwaku at the University of Maryland, College Park, MD. I am an international student from Nigeria with a strong commitment for excellence in research. My purpose as a researcher is to contribute immensely to the field of pharmacology and biochemistry for the principal goal of eradicating diseases while making the world a better place.

My research focuses on screening for small-molecules that bind viral and pathogenic RNAs by NMR using selective Isotopic labels. The underlying problem that gave rise to this research is the increasing rate of antibiotic resistance which is an health crisis that comes with a huge financial burden. With the emergence of new resistance mechanisms, there is the need for the discovery of more small molecules that can function as effective antibiotics. In this research, we aim to identify a library of small molecules that bind specifically to various RNA fragments (20-30 nt) using nuclear magnetic resonance (NMR) spectroscopy. Due to the sensitivity of NMR chemical shifts to the environment, this technique affords us the ability to identify whether the RNA is bound and what parts of the RNA is interacting with the small molecule(s). We are synthesizing these RNA fragments using a chemo-enzymatic labeling strategy developed in our group to effectively study large RNAs by NMR. This approach will be used for studying fragments and eventually the full-length RNA in complex with the ribosome. Findings from this research could help identify potential therapeutic targets for treating a variety of bacterial infections.My passion in this research is rooted in the fact that this and other related researches hold the key to closing the door behind the problems brought about by antibiotic resistance particularly in developing countries.

I studied chemistry at Goethe University in Frankfurt, Germany. During my master studies, I worked with biomolecules, namely RNA and proteins. I also worked with NMR for the first time and my interest in this field grew a lot. Therefore, I chose the topic of my master thesis to be the investigation of the dynamics of a chaperone-RNA-complex by NMR spectroscopy. I performed my thesis in the group of Boris Fürtig and it was such a great experience, that I decided also to do my PhD in his group.

My research focuses on the E.coli RNA-chaperone StpA and the understanding of its interaction with bistable RNA constructs. The driving force of the activity of StpA is unknown so far. I am investigating the effect of the protein on the thermodynamic, kinetic and dynamic properties of RNA refolding. Therefore, besides conventional 1H-based NMR, I use laser-assisted real time NMR experiments and want to employ CEST experiments to follow the conformational change in the RNA at atomic resolution. I like the combination of the biochemical synthesis of RNA and protein with the investigation of these biomolecules by NMR. Overall, it fascinates me, how we are able to follow the interactions of considerably large biomolecules with nuclear resolution on a remarkably small timescale.

I am a third year graduate student at the University of Colorado Denver Anschutz Medical Campus in the Structural Biology and Biochemistry program working in Dr. Beat Vogeli's lab. I grew up in Indiana and studied Chemistry and Microbiology at the University of Rochester, where I also was on the rowing team. When I am not in lab, you can typically find me skiing or mountain biking.

My research is fundamentally driven by wanting to know how substrate interaction leads to dynamic and structural rearrangements throughout a macromolecule. My current work is elucidating the allosteric network of the two-domain protein, Pin1, where binding in one domain influences the activity of the other through an interdomain interface. I am interested in determining what causes the inherent motion of a protein, and how these dynamics are critical for its function.

I received a B.S. in chemistry from the United States Naval Academy in 2008. After serving for six years and completing three deployments as a Surface Warfare Officer I transitioned out of the Navy, briefly working as a consultant before returning to graduate school at UC Irvine. My husband, Wyeth who is a graduate student in the Patterson lab at UCI, and I have a three-year-old rescue pug named Neptune. Outside of academics I enjoy doing game nights with friends, going on backpacking trips, almost anything to do with the ocean and dabbling in creative ventures. I am currently a Pedagogical Fellow at UCI and am excited to continue onto a career in academia.

My research project in the Martin Lab is on the design and construction of a triple-resonance switched-angle spinning (SAS) probe for the study and characterization of orientable media such as non-crystalline solids and membrane proteins. In the lab this will be used to study structures and aggregation pathways of eye-lens proteins that physiologically exist at very high concentrations as a hydrogel, and novel anti-microbials that we have identified from the carnivorous plant Drosera capensis. Recent focus has been on creating a generalizable approach to achieve optimized transceiver coil designs that will eventually be implemented into the SAS probe. This work has been accomplished by using multi-physics simulation software and 3D printing. In addition to my thesis work I have the opportunity to mentor undergraduate student researchers in several projects from characterization of carnivorous plant volatile organic compounds, to pigments that give rise to different colors in flowers. I am passionate about these interdisciplinary projects because I have had the opportunity to learn so much and grow as a scientist and mentor. I am grateful to be part of this community and to contribute to the future of NMR, which has a proud and extremely impactful history, while mentoring others in their own journey as scientists.

I am a fifth-year graduate student at the University of Miami under the supervision of Dr. Jamie Walls. My commitment to NMR is entirely due to the inspiration of my advisor during the first-year class he taught. I spent most of my spare time lifting, skateboarding and enjoying watersports as Miami is heaven for such recreations.

My research focuses on the fundamental understanding of spin systems and novel pulse design. I studied the breakdown of linear response theory under low-power excitation for both inhomogeneously and homogeneously broadened system. By comparing exact propagator and linear response approximated propagator, linear response theory failed to predict spectra features near the transmitter frequency even though the response was still in the linear region given the overall flip-angle is small. For spin resonances in the bandwidth of the RF pulse, increased interference between isochromats led to a negative spectral peak which was not predicted by linear response theory. This failure was due to the fact that the interaction cannot be treated as a simple perturbation for isochromats with frequencies inside the bandwidth of the RF pulse. More recently, I developed diffusion selective pulses (DSPs) that can selectively suppress the magnetization from species with a diffusion coefficient, D. The main design philosophy behind DSPs is the realization that diffusion in the presence of pulsed-field gradients (PFGs) leads to an effective T2 decay which depends upon D. Thus, a T2 selective pulse, which was efficiently approximated by several small flip-angle rectangle pulses, can be interwoven between a series of PFGs to suppress an effective T2 thus a particular D.

I am a Ph.D. student at Texas Tech University and a member of Dr. Latham’s group, which mainly studies protein structure and function. I received my bachelor’s degree in chemistry from the Sharif University of Technology, and I moved to the US three years ago to get Ph.D. in biochemistry. My goal is to pursue my career in academia and, one day, start my independent research.

Protein self-association is a common feature of some proteins and plays an important role in health and disease. Cleavage stimulation Factor (CstF-64) contains an RNA recognition motif (RRM) that binds to the G/U rich RNA sequences located downstream of the cleavage and polyadenylation site and hence its function is very crucial for the regulation of the RNA maturation. My current project is the study of CstF-64 RRM self-association and its conformational changes upon RNA binding with the use of NMR relaxation techniques. I believe the result of my project can help not only to explain the cleavage and poly adenylation process better but also to understand the mechanism of self-association in other RNA binding proteins.

Hi, I'm Seo-Ree Choi, first year of Ph.D student. I'm studying at Prof. Joon-Hwa Lee's lab at Gyeongsang National University in Korea. I love going to new areas in search of delicious food. And it's an honor to receive an ENC student stipends and be featured in the catalogue. Thank you for giving me great motivation for further research.

My research focuses on investigation of the interaction between DNA and DNA binding proteins using solution NMR. My current work is the dynamics of transcription factor proteins and target DNA. I will systematically conduct structural and dynamic research to identify the molecular mechanism between DNA double helix and transcription factors. I am interested in this research because there is a lot of information with NMR, and I like to acquire new things and teach my know-how to other graduate students.

As a PhD candidate in Prof. Garwood’s group in the University of Minnesota, I plan to become a Medical Physicist in a research based institution after graduation. I am quite interested in the potential use of MRI/NMR in the dosimeter and radiation oncology areas. In my spare time, I love baking and playing violin. I also volunteer as a caregiver and a foster at a local animal shelter.

My research focuses on building low cost, portable NMR imaging systems that can do simultaneous transmit and receive. Based on fictitious field principle, our system is a combination of novel spacial encoding and detection methods. It can achieve simultaneous transmit and receive with minimum leakage problem. One-dimensional imaging has been acquired with a resolution of ~2 mm. Two-dimensional imaging system is currently being built in our lab.

I am a third-year graduate student in Dr. John Franck’s lab at Syracuse University. I enjoy reading both scientific and non-scientific literature, writing, and drinking coffee.

My research strives to broaden the applications of liquid state Overhauser Dynamic Nuclear Polarization (ODNP) to glean information on hydration water dynamics in diverse chemical systems. While this technique has been used successfully to study proteins, its extension to the study of other systems such as reverse micelles is non-trivial. I am working to develop a systematic procedure for studying these different systems using this experimental technique. While my work will provide new insight in hydration dynamics, it is also a fascinating blend of NMR and EPR spectroscopies and pushes the limits of the information we can obtain with this dual-resonance technique.

I received my BS in chemical engineering from the University of Maryland, Baltimore County (UMBC). I am currently a PhD student at Georgia Tech advised by Carsten Sievers and AJ Medford. My long term goal is to become a faculty member focusing on heterogeneous catalysis for biomass conversion. In my free time I enjoy cycling, cooking, collecting records, and spending time with my friends and family.

I am interested in the transformation of biomass derived chemicals into platform chemicals using heterogeneous catalysts. I'm specifically interested in the interactions sugars have with metal oxide catalysts. By further understanding these interactions, selectivity and other important factors regarding the reaction route can be elucidated. These applications can revolutionize the way energy is processed around the world and provides a sustainable alternative. I am particularly drawn to this line of research because of the impact it can have on our society and the pressing need to protect our environment it addresses. As a chemical engineer, NMR in general is very under utilized in the field. My work using solid state NMR will hopefully show other chemical engineers in the field its capabilities and make it a more widely used technique.

I am a PhD student in Dr. Grandinetti’s group at Ohio State University currently in my fourth year. I received my B.Sc. at the University of Cincinnati in chemistry. In my free time, I enjoy hiking, swimming, and watching movies.

Since my first chemistry class in high school, I’ve been interested in learning about how atomic structure influences physical properties. My research focuses on improving the sensitivity of 29Si and 17O in silicate glasses in order to permit natural abundance multidimensional NMR measurements of these amorphous systems. Such measurements are necessary to learn more about the structure of these glasses because their distributions of sites introduce line shape broadening that complicates traditional one dimensional spectra. By gaining a better understanding of these systems, we aim to construct structure-property relationships that can be used to develop specialized glasses for specific functionalities.

I'm a 3rd year PhD student in the group of Dr. Anne Lesage at the CRMN in Lyon. I did a bachelor in Chemistry at St. Joseph University in Beirut-Lebanon before transferring to Lyon where I continued my studies at CPE and the UCBL1 to get my master's degree in innovative materials for transportation, energy and health.

My research focuses on the study of Heterogeneous catalysts using DNP surface enhanced NMR spectroscopy. By probing distances between pairs of nuclei I can get to the 3D structure of the catalyst in question and thus understand the stability and the efficiency of this catalyst. I can also get environmental information around the metal center using ultrawideline NMR to get a full understanding of this grafted catalyst. All the materials I work with are diluted on the surface and usually a blend of active and spectator species which makes the study more challenging and needs new and advanced methods to selectively probe certain nuclei on selective species. That's what makes it more interesting and more enjoyable. I'm passionate about this work because I have the chance to work with a state of the art technique (DNP), to develop new experimental ways of looking at your sample then compare it with simulations to get the full information and fully understand what's happening on your surface.

I am a PhD candidate at the National High Magnetic Field Laboratory at Florida State University studying biomedical engineering with a focus in high field MR imaging and spectroscopy. I received my bachelor's degree from Auburn University in cellular and molecular biology and my master's in biomedical engineering from Florida State University. Several additional years of experience as a technician specializing in animal models, mostly focused in neurodegeneration, has motivated me to work towards translational research incorporated into the MRI/S field.

The foundation of my research capitalizes on the potential of ultra-high field MR imaging and spectroscopy for non-invasively elucidating metabolism and function, a critical requirement for evaluating cellular therapies in neurodegenerative diseases. Specifically, I am interested in evaluating the optimization, expansion and delivery of human mesenchymal stem cells applied to a preclinical model of ischemic stroke using MRI/S. Increased sensitivity of 1H MRS at high field provides longitudinal metabolic mapping of biological markers in response to cellular treatment. Further, quantification of sodium (23Na) signal provides insight into cerebral ionic homeostasis and tissue recovery following ischemic stroke.

I am a Ph.D. student at Texas Tech University and a member of Dr. Latham’s group, which mainly studies protein structure and function. I received my bachelor’s degree in chemistry from the Sharif University of Technology, and I moved to the US three years ago to get Ph.D. in biochemistry. My goal is to pursue my career in academia and, one day, start my independent research.

Protein self-association is a common feature of some proteins and plays an important role in health and disease. Cleavage stimulation Factor (CstF-64) contains an RNA recognition motif (RRM) that binds to the G/U rich RNA sequences located downstream of the cleavage and polyadenylation site and hence its function is very crucial for the regulation of the RNA maturation. My current project is the study of CstF-64 RRM self-association and its conformational changes upon RNA binding with the use of NMR relaxation techniques. I believe the result of my project can help not only to explain the cleavage and poly adenylation process better but also to understand the mechanism of self-association in other RNA binding proteins.

I am a PhD candidate in the Utz group at the University of Southampton, UK. When I am not in the lab, I love to cook and crochet.

Microfluidic lab-on-a-chip (LoC) devices have a huge potential as they can integrate synthesis, separation, analytical techniques and biological cultures on a single portable platform. NMR is an ideal read out technique for LoC due to its non-invasivness, generality and the ability to extract rich metabolic data. My research focuses on integrating parahydrogen induced polarization (PHIP) with LoC to enable detailed observation of metabolic pathways. I am passionate about my research because I believe that it will transform research and development in the healthcare system.

I grew up in middle California and did my undergraduate studies in San Francisco, and followed this with a move to the East Coast where I currently reside in Washington D.C. My main accomplishments include playing guitar very poorly and spending most of my time out of lab backpacking in the Shenandoah mountain region.

I became interested in NMR spectroscopy in the context of observing the products of my failed organic chemistry reactions in fine detail. I figured that proteins would be more fun to study and easier to work with, so I moved to UMD with the aim of using NMR as a primary method to study structural biology aspects of ubiquitin signaling systems. And, as it turns out, the protein ubiquitin isn't just a NMR standard... As a junior scientist I have previously used unnecessarily large magnets to solve protein structures and study binding interactions, but recently my focus has shifted to studying the reaction kinetics of small molecules with ubiquitin. This includes both investigating transient carbamylation reactions on ubiquitin lysines, which directly influence cellular homeostasis, as well as studying the kinetics of ubiquitin 'activation' by the cognate enzyme which initiates many cellular processes. In both of these cases I utilized the unique ability of NMR spectroscopy to measure reaction kinetics while directly observing changes in the fine structural details of proteins.

I am a licenciate in Molecular Biology from the University of Buenos Aires, Argentina. In 2020, I started my PhD under the supervision of Dr. Daiana Capdevila at the Leloir Institute in Argentina, focusing on the molecular evolution of bacterial transcription factors, and the role in protein dynamics in their function. As Latinamerican PhD student, the travel stipend given by the ENC will allow me to present the results of my research to the scientific comunity for the first time, and for it I am deeply greatful.

As a molecular biologist, I am driven by my curiosity to understand the most fundamental processes that allow life to exist. One of the major threats that our species faces is the rapid increase in bacterial resistance to antibiotics, and we cannot understand how novel resistance mechanisms appear throughout evolution unless we understand the structural and dynamical properties of the proteins involved. In our lab, we study a family of bacterial proteins that regulate the expression of genes involved in the bacterial response to antibiotics and other forms of host-derived stress. We use NMR to assess how dynamical changes triggered by a ligand-binding event regulate the function of these proteins, hoping to unveil potential new ways to combat multi-drug resistant pathogens.

Follow this link to view our Lab Twitter.

I was raised in Syracuse, New York and plan to finish my graduate studies within the coming year. I plan to continue working in NMR. I find it an immensely fascinating field whose various applications never cease to amaze me. In my spare time I enjoy computer programming, reading and writing, and studying languages.

My research involves using solution state magnetic resonance to study the dynamics of water inside reverse micelles. Reverse micelles are essentially mixtures of water, oil, and surfactant. When present in the right ratio, the surfactant allows the water to be dispersed into the oil as tiny droplets, in essence enabling water and oil to "mix" which in the absence of surfactant would not happen. In a reverse micelle sample, water accounts for a very small percent of the overall volume. That makes detecting the water with respect to NMR a challenge, and subsequently my project deals with tackling that challenge while I am trying to study the water dynamics inside the reverse micelles. I use specifically deuterium relaxometry measurements as well as Overhauser DNP to study the water motion. Thus I find the project interesting from both an experimental and scientific perspective. Applications for this project deal with understanding water in confined environments, such as one might find inside cells in biology.

I am a 3rd year PhD student in biomedical physics who enjoys nerdy books (think Harry Potter, Game of Thrones, Lord of the Rings, etc.), playing piano, and relaxing with video games. My favorite color is green, I can solve a 5x5 rubik's cubs,  and mint-chocolate chip is the superior flavor of ice cream above all others, and I'll fight anyone who disagrees. Also I can't whistle.

I perform experimental research in biomedical physics in several diverse areas, including conducting NMR spectroscopic investigations of the metabolism of glioblastoma and neuroblastoma cancer, studying the temperature dependent decay of free radicals, and constructing and achieving dynamic nuclear polarization via the Overhauser Effect for the enhancement of NMR spectroscopy. Biomedical physics is the merging point of a variety of STEM fields such as chemistry, biology, physics, and engineering, and to me is a beautiful way to be able to learn about and experience all of these wonderous disciplines. This in conjunction with the knowledge that I'm performing research that can advance the medical field and potentially help people and save lives gives an extraordinary sense of fulfillment and joy in my work. Plus, I get to play with expensive, fancy science toys!

PhD Candidate at Karlsruhe Institute of Technology in Germany (Institute for Microstructure Technology)

Can we enhance traditional algorithms used in NMR with artificial intelligence methods? I am passionate to bring the success of deep learning (seen in fields like computer vision) to the NMR community, in order to make the research itself easier and faster.

As an international student it was a great honor for me to be admitted into The Department of Chemistry and Biochemistry at Texas Tech University. The Ph.D. program in the Department of Chemistry and Biochemistry provides me with unique opportunities to advance my scientific breadth and hone my science communication skills by acting as a teaching assistant for courses including general chemistry lab, physical chemistry lab I and II.  Most importantly, TTU allows me to work with Dr. Benjamin J. Wylie, who is an outstanding advisor and researcher. Dr. Wylie taught me how to design new radio-frequency pulse sequences for Solid State NMR.  These new techniques will allow me to study biomolecules on the biologically relevant micro to milli second timescale. Specifically, we are applying these techniques to large membrane proteins in biologically-relevant environments. I have characterized a large membrane protein, KirBac1.1, via Solid State NMR. This is an important achievement not only because KirBac1.1 is a membrane protein that transports potassium ions through the membrane, but it is 1.72 times bigger than any other protein that has ever been fully characterized via Solid State NMR. I was able to publish my first paper as the first author in the outstanding journal of Proceedings of the National Academy of Sciences of the United States of America (PNAS), “Conformational changes upon gating of KirBac1.1 into an open-activated state revealed by solid-state NMR and functional assays” December 2019. I am also co-first author on the other paper published in the outstanding Journal of American Chemical Society (JACS), “The lipid activation mechanism of a transmembrane potassium channel” July 2020. I was able to publish another paper as the first author in the outstanding journal of Frontiers in Molecular Biosciences, “Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State” November 2021.My father died from a heart attack fifteen years ago. He was a taxi driver who did not finish high school; I always tried to make him proud of me. Today, I am studying K+ channels involved in the inner machination of the heart. That is why I think Texas Tech University is a place where a father will be proud of his son.

My research focuses upon solid state NMR, membrane proteins, and lipid bilayers.I used SSNMR to characterize the KirBac1.1 potassium channel in both the open activatedand closed-inactivated state. I assigned ~90% of the 15N and 13C resonances in both states of the channel. This work was carried out at a modest 600 MHz B0. This detailed analysis was enabled by both the sensitivity gained from non-uniform sampling (NUS). Reza uncovered a chemical shift perturbation (CSP) pattern revealing a novel allosteric pathway between the activation gate and the selectivity filter. My discovery indicated that rectification via anionic lipid binding induces conformational changes resulting in two different conformers in the activated lipid composition. I hypothesized that these conformational states are responsible for fast-gating phenomena. This first study was published in PNAS in early 2020.Following this study and, I leveraged my chemical shift assignments to determine the water accessible surface of KirBac1.1 in the activated and inactivated state. Surprisingly, I found that the water-accessible surface of KirBac1.1 is much larger in the inactivated state compared to the activated state. These measurements indicated the gating paddles of KirBac1.1 twist to form tight contacts in the activated state. This work was published in JACS in mid 2020.Now I am focused on solving the atomic-resolution structure of KirBac1.1 in the heretofore unknown open-activated state. SSNMR structures of membrane proteins are often hampered by poor chemical shift dispersion and internal dynamics which limit resolved distance restraints. However, the ordering and topology of these systems can be defined with site-specific water or lipid proximity. Membrane protein water accessibility surface area is often investigated as a topological function via solid-state NMR. For the first time, I used water-edited solid-state NMR measurements in simulated annealing calculations to refine a membrane protein structure. He developed this new protocol in collaboration with Dr. Charles Schwieters at NIH. Then I demonstrated the power of water-accessibility structural restraints by refining the full-length structure of KirBac1.1 in the closed state. Reza is now solving the structure of the open-activated state of KirBac1.1 by applying water-accessibility restraints along with distances from CCC 3D experiments acquired at 900 MHz and interpreted with a new three-dimensional PASD module within Xplor-NIH.

I am from Chittagong, a port city of Bangladesh. I completed my undergraduate study in 2011 from Noakhali Science & Technology University, Bangladesh and my major was Applied Chemistry & Chemical Engineering. In November 2011, I moved to Munich, Germany to pursue my master's in advanced Materials Science from Technical University Munich. After my masters, I worked for Intertek( Bangladesh) and GlaxoSmithKline (Bangladesh) for several years. In spring 2019 I have started my graduate school at Southern Illinois University Carbondale (SIUC). Currently I am working at Dr. Boyd Goodson research lab and serving as a member of NMR facility operation and maintenance team at SIUC.

We are a NMR/MRI research group works on hyperpolarizing various biologically active molecules by using (1) spin-exchange optical pumping (SEOP); and (2) parahydrogen induced polarization (PHIP) such as SABRE (Signal Amplification by Reversible Exchange) methods that suffers from poor detection sensitivity.  In our research group my focus is mainly synthesis & development of novel MOF-based heterogeneous SABRE catalyst which will help the effective separation of hyperpolarized substrate molecules of various biological interests from the catalyst solution.

I am PhD Candidate in the field of physics on the Faculty of Physics and Applied Computer Science at the AGH University of Science and Technology. I have been dealing with NMR since the engineering diploma practices in 2015. After getting acquainted with the basics of the method and conducting experiments on models, I started to work in the STRATEGMED2 research grant from the National Centre for Research and Development under the supervision of dr. Artur Krzyżak connected with evaluation of the clinical WJMSCs potential in selected cardiovascular diseases using novel MRI methodology. I realized how little NMR potential is used in everyday use, e.g. in medicine or petrophysics. Therefore, in my doctorate, I decided to focus on increasing the applications of NMR and MRI by delivering practical tools for researchers from different fields of study. I like that my work is highly interdisciplinary, requiring an understanding of a scientific problem in a non-physics field. I am also passionate about overcoming well-known experimental problems. Currently, I work in the Medical Research Agency research grant under the supervision of dr. Artur Krzyżak connected with improving diffusion tensor imaging of the brain of a patient with SM.

My research focuses on accurately characterizing the porous microstructure using nuclear magnetic resonance (NMR). The pursuit of this is sometimes hampered by technological limitations, but some obstacles can be overcome with proper workflow or post-processing. In NMR imaging (MRI) one of the problems regarding the accurate porosity characterization is the presence of systematic and statistical errors. I aim on the reduction of these errors in order to minimize the MRI parameters shifting and improve microstructure visualization. What I am passionate about in my research is that porous structures are present almost everywhere, from rocks to tissues, while NMR is superior non-invasive method to reflect their geometry and physicochemical properties. This makes this method universal and I find very rewarding delivering new NMR/MRI applications or methodologies to researchers in fields other than physics to support their studies. Additional satisfaction comes from improving MRI techniques with the verification in simulations and, consequently, increasing their usability.

I am a Ph.D. candidate in the Dr. Andre Simpson research group. My research focus is on Environmental Chemistry. When I am not working on my research, I spend much of my time volunteering in my community. During my Ph.D., I have started and hosted multiple events aimed at improving the professional development experience of graduate students. I also host social events to improve the graduate student experience on campus. Outside of the university I volunteer with non-profit organizations to teach chemistry in low-income communities. I have also committed to spending my time mentoring young girls in the community to encourage physical activity and discussions on mental health. In my personal time I enjoy travelling, reading, and running!

My research focuses on bridging Nuclear Magnetic Resonance (NMR) Spectroscopy with Metabolomic studies to address environmental problems at the molecular level. My approach is to develop in-vivo NMR techniques that provide the ability to monitor living organisms at the biochemical level in real-time. During NMR studies stressors can be introduced into the organisms' environment while they are inside the NMR magnet and any perturbations to underlying metabolites can be correlated to biochemical pathways to explain why a chemical is toxic. As the organisms are kept alive during these studies, temporal studies can follow to determine if a response is a temporary flux or a permanent change to the organisms' biochemistry - the latter a likely precursor to disease and a clear signal for policy-based decisions. My research uses keystone species which could impact the functioning of ecosystems. By understanding their response to stressors they act as an early warning sign and identify issues prior to larger scale threats to population dynamics and ecosystem shifts. My research allows me to combine my passion for chemistry with my love for the environment and making sure we are taking care of our only home!

I am a PhD candidate at University of Grenoble Alpes, France going to graduate in summer 2022. I am originally from Zagreb, Croatia where I did my bachelor and master studies at the Department of Chemistry, University of Zagreb. While living in Grenoble, I discovered love for the mountains and learned a lot from a dynamic structural biology community at the campus.

The project I am working on during my PhD training is focused on elucidating the sequence of events during the first steps of the mitochondrial protein import. Mitochondria play a central role in  numerous cellular processes with 99% of their ~1500 different proteins encoded by the nuclear genome and synthesized in the cytosol. These precursor or client proteins include carriers of the inner mitochondrial membrane, outer membrane pores and membrane anchored proteins, along with matrix and intermembrane space targeted protein. Mitochondrial function depends on correct localization and fold of these precursors, emphasizing the importance of the post-translational import conducted by the mitochondrial import machineries. Our main research is focused around studying the complexes of mitochondrial precursor proteins with the different players of the import pathway, mainly the cytosolic receptor domains and intermembrane space chaperones. We are applying a set of biophysical methods with the aim of characterizing these low affinity, and often highly dynamic complexes, and in our work we mainly rely on solution NMR spectroscopy as an excellent method not just in solving the proteins structure but also in studying proteins dynamics whether in its apo- or client-bound state, affinity towards the client and characterization of the binding interface. This project, started in the Biomolecular NMR Spectroscopy group at IBS, Grenoble, is undergoing in the Prof. Paul Schanda’s group at IST, Austria.

I am a 4th year physical chemistry Ph.D. student at Iowa State University. My hobbies include snowboarding, playing guitar, hunting, fishing and spending time with family and friends.

My graduate research under the supervision of Prof. Aaron Rossini at Iowa State University focuses on (1) the development of solid-state NMR spectroscopy pulse sequences and (2) the use of solid-state NMR spectroscopy for the structural characterization of materials, such as insulating or semi-conducting two-dimensional nanomaterials and nanocrystals, mesoporous materials, polymers, and heterogenous catalysts. It is really interesting to probe/determine the chemical structure of novel materials because it provides critical information to rationally design and develop next-generation materials. I greatly enjoy developing and performing solid-state NMR spectroscopy experiments because NMR is extremely sensitive to changes in local chemical structure and is one of few techniques capable of providing atomistic descriptions of dilute surfaces, edge sites and catalytical active sites.

I am a 4th year chemical engineering PhD student working in the Messinger Lab at The City College of New York. I am originally from Scotland, and attained my Master's degree in Chemistry from the University of Edinburgh, where I worked on electrochemical sensors. Upon moving to New York for graduate school in 2018, I joined the Messinger group to work on NMR of energy storage systems. In my free time I like to go bouldering, and I love cooking and baking.

I work on metal-anode-based battery systems, using a combination of solid-state, and liquid-state NMR techniques to elucidate charge storage mechanisms and performance enhancements. With this work, we hope to develop rigorous understanding of both multivalent-organic batteries, and of improvements to liquid electrolytes for lithium metal batteries. I deeply enjoy the challenge and opportunities offered by magnetic resonance spectroscopic techniques and I love coupling that with the important goal of attaining a low emission and renewable energy future.

Mohammad Shah Hafez Kabir has completed his Bachelor of Pharmacy in 2015 from International Islamic University Chittagong, Bangladesh. He is now a Ph.D. candidate at the Department of Chemistry, Wayne State University, USA. He has founded the GUSTO A Research Group in 2014, which is a non-profit research organization. The purpose of the GUSTO is to help young undergrad students to conduct research in their fields. From 2014 to 2018, he had done his research on the biological activity of different plant extracts, drug-drug interaction, bioinformatics, and ovarian and breast cancer. During the 4 years of his Ph.D. (September 2018 to now), he has been doing his research on several chemically active compounds (metronidazole, fluoro-metronidazole, nimorazole, fampridine) for screening their hyperpolarization profiles. He has also performed several ab initio calculations to understand nitroimidazole-based antibiotics metabolic reduction process due to hypoxia, and SABRE polarization transfer pathway through Ir-based catalyst. He has made different YouTube videos to explain numerous scientific topics and methods. Kabir has received many awards for his research excellence at several scientific conferences.

Magnetic resonance imaging (MRI) is a non-invasive technique to detect hypoxia. During MR imaging, a contrast agent is used, where hyperpolarized (HP) contrast agents can increase the imaging quality. Hyperpolarization techniques increase the polarization of nuclear spins by 4-5 orders of magnitude over the conventional thermal (Boltzmann) polarization level, so hyperpolarization leads to corresponding large improvements in MRI detection sensitivity. During the 4 years of my Ph.D. (September 2018 to now), I have used several chemically active compounds (metronidazole, fluoro-metronidazole, nimorazole, fampridine) for screening their hyperpolarization profiles. We used HP contrast agent 15N3-metronidazole with large 15N polarization, long lifetime of 15N HP state, and biological relevance. We use the hyperpolarization method called Signal Amplification By Reversible Exchange in SHield Enables Alignment Transfer to Heteronuclei (SABRE-SHEATH). Metronidazole structure contains a nitroimidazole moiety. In hypoxic conditions, it would undergo electronic reduction, and the -NO2 (nitro) group reduces to a -NH2 (amino) group. I have also examined Metronidazole, fluoro-metronidazole, nimorazole, and their putative metabolites by ab initio calculations. My aim is to establish HP metronidazole as a novel contrast agent for MRI technology for hypoxia sensing.

Most people know me by my middle name “Charya.” I am from Colombo, Sri Lanka (a pear-shaped island located just few miles away from South India). I received my B.S. in Chemistry (with minor in Plant Biology and Management Science) in 2017 from University of Sri Jayewardenepura, Sri Lanka. Currently I am pursuing my PhD in Department of Chemistry at LSU, Baton Rouge under the supervision of Dr. Megan Macnaughtan. Experiences acquired daily through research inspire me to explore more in bioanalytical field. Apart from academic studies, I would love to spend my time in travelling, meeting new people, making new friends, trying different cuisines, and exploring diverse cultures.

The Chlamydia trachomatis chaperone protein, Scc4, is a unique protein that plays a vital role in Chlamydia pathogenesis. The bifunctionality of Scc4 to act as an RNA polymerase binding protein and a type III secretion system (T3SS) chaperone provides an advantage as a therapeutic target. Scc4 has a dynamic structure until it binds its T3SS chaperone partner, Scc1. The structure of Scc4 shows a dramatic change upon binding Scc1 suggesting that the bifunctionality is the result of a conformational switch (Ukwaththage et al., 2020). We are determining the structures of Scc4 and the Scc4:Scc1 complex using nuclear magnetic resonance spectroscopy (NMR) to better understand the switching mechanism. Drug discovery will also be pursued using the backbone resonance assignments of both targets to screen for small molecule binding.

I’m a final year Ph.D. candidate in the Physical Chemistry group at Louisiana State University, Baton Rouge, LA, soon to be graduate.

My research project in the Tuo Wang Lab is on the model assembly of carbohydrates in pathogenic fungal cell walls under internal and external stress conditions. Initially, I found that the cell wall of A. fumigatus was found to contain hydrophobic scaffolds of chitin and α-glucans, which are surrounded by a hydrated matrix of β-glucans and capped by a dynamic layer containing mannan and galactan-based polymers as well as glycoproteins. Second, ssNMR results of carbohydrate-deficient mutants revealed how the gene deletion induces significant changes in the composition and water accessibility of biopolymers. Lastly, we identified a structural mechanism by which fungal pathogens regulate cell wall remodeling in response to antifungal drugs and environmental stresses. Collectively, these three studies provide a structural basis for designing better antifungal medications targeting the structure and biosynthesis of cell wall components. I am passionate about this research because carbohydrates are spectroscopically (NMR) beautiful.

I am a PhD student in Dr. Steven Suib’s group in the Chemistry Department at the University of Connecticut. I received my B.Sc. In chemistry and mathematics from Creighton University in Omaha, NE in 2015.

My research involves studying manganese oxide polymorphs via ssNMR. Manganese oxides are common battery materials that contain various tunnel sizes which can incorporate ions. While other characterization techniques are limited to the surface of the particle or by particle size, NMR reveals the bulk of the structure. I am specifically interested in nsutite and ramsdellite materials that contain 1x2 tunnels, which are difficult to characterize due to microtwinning. By probing the framework directly instead of the tunnel cations, we are able to more accurately characterize our battery materials.

I am a PhD candidate in the Frydman group in Weizmann Institute of Science. I grew up in Jerusalem and received my bachelor's degree in chemistry from the Hebrew University. I attained my master's degree from Weizmann Institute of Science. In my free time I like to read, create collages and run.

My research focuses on new methods in solid-state NMR in order to improve the sensitivity and information-content available.  The application of optimized data acquisition protocols can greatly facilitate the acquisition of solid-state NMR data. In this context, we investigated the use of steady-state free precession (SSFP) experiments in high field solids NMR and its ability enhance the sensitivity of wideline spectra. Additionally, I explored a new 2D correlation approach applicable for quadrupolar isotopes under static conditions, Quadrupolar Isotope Correlation SpectroscopY (QUICSY), which could aid in assignment of overlapping sites. Recently, I am studying a novel CEST-like experiment in solids that we term Progressive Saturation of the Proton Reservoir (PROSPR), for the detection of dilute and unreceptive spin species in solids. I am always fascinated by the possible depth of solid-state NMR and the richness of experiments and details you can learn by this method.

I have been in the lab since 2017 and have been doing nmr research for 5 years. I am using nmr to conduct interesting research, including protein-DNA interactions, protein dynamics, and nucleic acid dynamics. So, I hope to become a good researcher through interesting research results in the future.

I'm doing research to measure the dynamics of nucleic acids with nmr. These studies are expected to play an important role in identifying the DNA recognition mechanism of transcription factor proteins or the biosynthesis mechanism of microRNA.

I finished my bachelors in chemistry in Ghana and then moved to US to continue with graduate studies. Apart of science, I love reading especially philosophy and history of science. When I’m not occupied with science and reading, I love to play soccer.

MRI is one of the most significant medical advances of the century. However in order to get clinically relevant data from MRI, very expensive MRI machines are needed. This is because of the large magnets used by MRI machines to polarize the protons found in the patient’s body. Without this larger magnets for polarization of the protons, the signal from the MRI is low and not useful. To deal with this problem, the technique of hyperpolarization using parahydrogen can be used to polarize molecules which can then be introduced into patients to act as contrast agents. By the use of these contrast agents, we can get better images with less expensive and sophisticated instruments. My research is on the building of instruments that can prepare hyperpolarized contrast agents on a clinical scale using parahydrogen.

Hi, I'm a PhD student from Department of Chemistry, Western University, Canada, under the supervision of Prof. Yining Huang. I obtained my bachelor degree in Materials Physics at University of Science and Technology Beijing, China and master in Applied Physics at University of Tsukuba, Japan.

My research involves using the solid state NMR to study the quadrupole nuclei in metal organic frameworks. I'm working on the 63/65Cu, 91Zr, 67Zn, 47/49Ti NMR studies and find them really interesting to explore the atomic level mysteris in MOFs.

I am a Ph.D. candidate in the department of chemistry at New York University. My research focuses on 31P NMR relaxation theory and nuclear spin singlet states. When not working on my research, I enjoy pursuing a variety of hobbies, including playing the piano, visiting museums, and attending concerts. My love of music and the arts is evident in the way I approach my research, as they always bring a creative and innovative perspective to my work in the lab. With a passion for both science and the arts, I am a person who is always looking for new ways to learn and grow.

My research focuses on the use of 31P NMR to study the magnetic properties of phosphorous-containing molecules. Specifically, my work involves the application of relaxation theory and nuclear spin singlet states to gain insight into the dynamics of these molecules in solution. I also employ two-dimensional diffusion-ordered spectroscopy (DOSY) as well as chemical exchange saturation transfer (CEST) explore the mechanisms of phosphate aggregation in common aqueous solutions.The overall objective of my research is to further our understanding of the behavior of phosphorous-containing molecules in solution, and to develop new methods for our analysis. By combining multiple NMR techniques, I aim to gain a more complete picture of the molecules being studied, and to provide a more comprehensive analysis of their properties. Ultimately, my research has the potential to lead to new insights and discoveries in the fields of biochemistry, medicinal chemistry, and materials science, among others.

Austin Browning is a graduate research assistant at North Carolina State University under the tutelage of Thomas Theis in the field of SABRE Hyperpolarization. Austin Browning was born in Asheville, North Carolina and received his undergraduate degree at Appalachian State University where he researched microwave assisted organic reactions and received his bachelor’s in chemistry with a minor in biology. He plans to earn his PhD of Physical Chemistry in December 2023 and is planning to pursue a career in industry or a startup company.

The research performed at the Hyperpolarization Lab at NCSU under Dr. Thomas Theis focuses on employing the hyperpolarization technique Signal Amplification By Reversible Exchange (SABRE). Recently, we successfully detected SABRE polarized 1-13C pyruvate in vivo, marking the first time SABRE has successfully been used for in vivo imaging. With these advancements, SABRE is positioned to become a leading hyperpolarization technique. Pushing novel technologies toward clinical applications is my primary motivator and the research I have performed at NCSU has pushed me towards this goal.

I grew up in rural Indiana and went to Purdue University where I got my bachelor's degree in 2016. Currently, I am a 4th year PhD candidate in the Tierney Lab at Miami University. For work I love big magnets, but when I am off work I love playing with my dog Roxy, climbing in the rock gym, dancing with my fiancée, and baking sourdough bread.

My research is focused on measuring the electronic characteristics of high-spin Co(II) complexes in solution. We use NMR, EPR, X-ray crystallography, and DFT calculations in order to extract a complete image of our samples. I am passionate about the instruments that we get hands-on experience running and (sometimes) helping fix. The spectrometers, diffractometers, and supercomputers we use are fascinating, and I work my hardest when I am learning about the instrumentation or software implementation.

I am a PhD student at the Department of Chemistry, University of Cambridge, England working in the lab of Prof. Dame. Clare Grey. My work focuses on extending the lifetime of very high energy density lithium air batteries. Recently I have been using operando 17O NMR to study the formation of breakdown products in the cell as it cycles. Outside the lab I enjoy hiking, bouldering and church bell ringing.

Lithium air batteries are a promising replacement to the ubiquitous lithium ion batteries. They have the potential for energy densities an order of magnitude higher than lithium ion, while avoiding using transition metals in their cathode. However, they are very short lived due to breakdown products form during cycling. Operando 17O NMR is an excellent technique to study this breakdown as it provides a real time, non-invasive way to study the formation and removal of these breakdown products, both in solid and solution state. My work initially focused on achieving sufficient signal to noise for operando measurements to be useful by using DFS/CPMG and enriched 17O2 gas. It then moved on to testing potential additives or cycling procedures in order to limit the amount of degradation products formed.

I am an MD-PhD candidate at Duke University currently working in the Warren Lab on SABRE hyperpolarization. I got my bachelor’s degree in chemistry and applied math at Davidson College where I played basketball. After defending my thesis in spring 2023, I will return to medical school and apply to residency programs in internal medicine with an eventual focus on pulmonology and critical care. Outside of science and studying, I enjoy staying active and will run, bike, and go rock climbing in the Appalachian Mountains in my free time.

My work focuses on hyperpolarization for applications to metabolic MRI. The inherently low sensitivity of MR techniques has limited the scope of measurable targets in the human body, but hyperpolarization techniques like DNP and SEOP are already being used to expand clinical imaging. I primarily focus on Signal Amplification By Reversible Exchange (SABRE) a cheaper and simpler alternative to solution state hyperpolarization via DNP. My research is centered around furthering our understanding of the dynamics governing the low-field variants of this technique where all nuclei are strongly coupled. In this regime, the J couplings, resonance frequency differences, and exchange rates are all on the same time scale which complicates analysis. I am passionate about this project because metabolic imaging has the potential to revolutionize the use of MRI in clinical diagnostics. Development of SABRE as an adjunct technique would increase the overall accessibility and portability of this diagnostic modality.

I am pursuing Ph.D. at Michigan State University under the supervision of Dr. Tuo Wang. I completed my Undergraduate and Master's studies in chemistry at Prairie View A&M University, Texas.

My research is focused on characterizing the fungal cell wall to the atomic level and comparing the cell wall in different fungal strains using Solid-state NMR (ssNMR) and Dynamic Nuclear polarization (DNP) techniques. I am passionate about investigating the remodeling of the fungal cell wall in response to the antifungal effect. The purpose of my study is to decode the structural contribution to virulence and provide the foundation for novel drug discovery.

I am a PhD student at the department of Chemistry at the Technical University of Denmark. I come from the south of Italy, then moved to the north of Italy and Paris, France, to pursue my Bachelor's degree. Then I moved once again to Denmark to get my Master's degree at the University of Copenhagen. There I specialised in NMR to study enzymes structure and molecular dynamics. Now, in my PhD project, I apply NMR and hyperpolarized NMR tools to decipher whole-cell catalysis. When I am not in the lab I am either at the gym or in some jazz club in Milan or Copenhagen. I love good music, opera, travels and history of art.

The central metabolism of microbes is an important resource for the future sustainable bio-production. A deep understanding of central metabolism and more extended reaction networks would accelerate and ease the production of chemicals through whole-cell catalysis. Usually, the modification of in-cell metabolism is achieved by adding catalysts through genetic engineering. Another unexplored way to modulate the natural central metabolism is the use of effectors and substrate mixtures. In my research I use NMR and DNP-NMR for in-cell tracking, to advance mechanistic insight and to optimise biochemical pathway usage toward the green production of chemicals.

I am a student of the last year of doctoral studies at AGH in the discipline of physics. I have been dealing with experimental NMR for 8 years. In my free time I like dancing, strength training, traveling and spending time with my fiancé and our dog. Music accompanies me both at work and at home or in the city. I am an addictive series watcher.

My research work focuses on new NMR applications to describe the pore space of materials found in biology, medicine, materials science and geology. They aim to characterize the microstructure and properties of these materials. In addition, I develop and apply methods that improve the quantitative analysis of NMR measurements, which I adapt to the type of material tested. Thanks to this, it is possible to improve the diagnosis of diseases, support translational medicine and accurately characterize pore systems in a non-invasive way, which is often unattainable using standard methods.

I am a Physics PhD candidate at the University of Texas at Dallas under Dr. Lloyd Lumata. I chose to pursue a PhD because the process of research is inherently engaging and fascinating. I chose Biophysics because imaging is interesting and I enjoy the multidisciplinary work. When I am not in lab, I enjoy video games and reading science fiction or fantasy novels.

Galactose is a glucose isomer which is processed, primarily in the liver, through the Leloir pathway. Interestingly, under hypoxic conditions, liver cancer cells seem to significantly reduce galactose consumption through glycolysis in favor of glucose alone. I am excited to use multiple new techniques to understand and detail this observation

I am a fourth year PhD candidate in biophysical chemistry in the Murray Lab at UC Davis. I received my bachelor’s degree in chemistry at Westmont College, where I ran track and cross country alongside my studies.

I study biomolecular molecules and their assemblies to understand the interplay between protein order and disorder in functional and disease states. We use a variety of analytical techniques to probe these native or misfolded proteins and their assemblies with an emphasis on solid-state and solution state NMR. Overall, this research hopes to better understand protein behavior at atomic resolution within these molecules.

Hi, my name is Qingqing (Emily). I completed my undergraduate studies in Pharmaceutical Science at China Pharmaceutical University. Currently, I am pursuing a Ph.D. in the Department of Biochemistry and Molecular Biology at the University of Florida. Apart from my research work, I enjoy volunteering at local pet shelters and experimenting with new recipes in the kitchen. I also have a love for outdoor activities, particularly hiking and drifting.

My research is centered on characterizing protein structural dynamics using solution NMR and DNP-enhanced solid-state NMR. I am particularly passionate about this area of study because NMR techniques provide powerful insights into amyloidogenic proteins, both in their monomeric and aggregated amyloid forms. Our recent research has shown that the amyloid material formed by the protein I am studying facilitates the detachment of biofilm on the tooth surface, which has implications for the development of preventive measures against human dental caries. I find this aspect of my work especially rewarding, as it has the potential to positively impact public health.

I am a graduate student at the Integrated Program in Biochemistry in University of Wisconsin-Madison, and working in the lab of Prof. Silvia Cavagnero. I enjoy listening to music and cat petting.

My research focuses on enhancing NMR sensitivity and applying LC-photo-CIDNP, which is a hyper-polarization NMR technique, to study protein folding and aggregation at low sample concentration.

Originally from Worcestershire, United Kingdom, I completed my MChem at the University of Edinburgh in 2019, during which I spent a year doing a research project at the University of Hong Kong. I then worked as a process chemist, working on pilot plant scale-production of small molecule pharmaceuticals, before starting my PhD in the Department of Chemical Engineering and Biotechnology at the University of Cambridge in January 2021. Normally, you can find me out and about exploring Cambridge whenever I can, or pretending I can run (I can't).

My research involves studying the application of MRI and low-field NMR to biopharmaceutical development. Using MRI, I am imaging components of commonly used perfusion bioreactors, in order to visualise and understand the hydrodynamic behaviour within them. With low-field NMR, I am using relaxometry to obtain key characteristics of biopharmaceutical solutions and cell culture media, and seeing whether we can bring this to the production line. Although I am an organic synthetic chemist by training, I have always had a bit of a soft spot for biology - this project gives me the chance to get hands on with something that I have always wanted to do, while potentially having a real-world impact in biopharmaceutical production!

I am a Ph.D. Student at the Institute of Medical Biochemistry of the Federal University of Rio de Janeiro, and work at the NMR Laboratory (CNRMN/Cenabio) under the orientation of Prof. Ana Paula Valente. I like to work with NMR techniques and my goal is to specialize in the characterization of biomolecules by NMR.

My research is focused on characterizing the protein structure and dynamics using liquid NMR techniques. For this work, I use the TTHA0849 protein from Thermus thermophilus. The structural dynamics are essential for protein function and Differences in forces that stabilize the structure of thermophilic proteins are subtle when compared to mesophilic proteins, which makes TTHA0849 a very interesting target for structural study.

I am a 2nd year Ph.D. student under the supervision of Prof. Sami Jannin at the Center of Nuclear Magnetic Resonance at the Université Lyon 1, France. Previously, I obtained a Bachelors degree in biochemistry and Masters in analytical physical chemistry, during which I developed the passion with NMR spectroscopy and hardware design. In my spare time, I enjoy hiking, cooking, and particularly traveling - where I love trying cuisine from all around the world. Otherwise, I can mostly be found taking silly pictures of my cat!

My work focuses on hyperpolarization using Dissolution Dynamic Nuclear Polarisation (d-DNP) that was introduced more than twenty years ago, and now provides a 10’000-fold gain in sensitivity on a routine basis. However, the experiment is in a single-shot manner, therefore mostly incompatible with NMR spectroscopy, ruling out for example phase cycling and multidimensional sequences. My Ph.D. project aims at turning d-DNP into a new version that will be widely compatible with NMR spectroscopy by replenishing hyperpolarization with a compact closed-loop freeze, melt, and flow system. This approach would also benefit the use of hyperpolarized NMR for reaction monitoring.

I am a M.S. student at Bucknell University, and received my B.S. from Lycoming College. In my free time, I enjoy oil painting, reading, and roller skating!

My research is focused on improving sampling schedule design in nonuniform sampling (NUS), and application of these schedules to make NUS of complex and cutting-edge 2D-NMR experiments more accessible to the community. We are working to identify and overcome the barriers to implement sparser 1D-NUS; increased sparsity in 1D-NUS correlates to repeat sequences in sampling schedules which lead to greater sampling noise and aliasing in resulting spectra. We address this through metrics which provide a better understanding of repeat sequences and inform the design of robust schedules.

I am currently a second-year PhD student in the Laboratoire des Biomolécules at the Ecole Normale Supérieure, Paris. I obtained my M.Sc. in Chemical Biology at the Karlsruhe Institute of Technology in 2019.

Long-lived states (LLSs) are spin states that can have lifetimes longer than the longitudinal relaxation time T1. Their lifetimes can also be strongly affected by changes to their magnetic environment, making LLSs sensitive to intermolecular interactions. The aim of my project is to use long-lived states to probe and characterize binding between ligands and proteins.

I am a 2nd year PhD student in Prof. Emsley’s Laboratory of Magnetic Resonance at EPFL, Switzerland. I was born and grew up in Moldova, but later moved to Strasbourg where I received both my B.S. and M.Sc. in Chemistry. I enjoy cooking, knitting, and listening to audiobooks.

I work on the development of a proton-based structure determination methodology in amorphous and crystalline molecular solids, such as small organic and pharmaceutical molecules, using ultra-fast magic-angle spinning (MAS) solid-state NMR. Today NMR crystallography mostly relies on the data obtained from 13C-detected experiments, which require isotopic enrichment and/or dynamic nuclear polarization to achieve sufficient sensitivity. Due to its high gyromagnetic ratio and extreme abundance, 1H NMR can be an attractive alternative, if the resolution of 1H solid-state MAS NMR could be improved by overcoming the large dipolar broadening.

I completed my bachelor’s degree at the Institute of Chemistry Ceylon, Sri Lanka and I am currently a PhD student in Chemistry in the Goodson Lab at Southern Illinois University Carbondale. Our lab is primarily an NMR lab studying hyperpolarization techniques. My hobbies include gardening, learning new languages, and watching historical documentaries.

Low-field MRI has the potential to address many limitations presented by conventional MRI when combined with hyperpolarization. My research involves integrating parahydrogen-based hyperpolarization techniques with a point-of-care 64mT low magnetic field MRI scanner. My work involves altering pulse sequences to obtain faster SABRE images in fringe fields either by transferring manually or by using a continuous liquid flow system which is then used to quantify sabre enhancements by comparing gray scale signal intensities to standard water samples. I am also involved in efforts to synthesize biologically relevant molecules to be used as SABRE substrates. We are currently working on building a continuous flow system to perform low-field MRI with HP propane gas.

I am a Ph.D. student at the Department of Chemistry, Seoul National University. I am interested in investigating biomolecular processes in native contexts for which I feel passionate about NMR. I enjoy developing pulse sequences and my goal is to develop new NMR methods to accurately analyze biomolecular systems in a physiological environment. In my free time, I enjoy cooking, listening to music, and spending time with cats.

My research focuses on investigating realistic states of proteins under a complex network of interactions in a cellular environment. I study conformations, dynamics, and modifications of intrinsically disordered proteins (IDPs) in cells. IDPs play central roles in many biological processes and diseases, although their intrinsic roles are largely unknown. I pursue deeper understanding of IDPs by investigating their in-cell specific properties which are not found under in vitro conditions.

I enjoy playing badminton on my free time. I also love to cook and make crafts at home.

My research focuses on the structural study of peptides that plays an important role in the innate immune system of insects. These peptides may interact with EGFR-like molecules and the study may aid in the development of potential EGFR inhibitors useful in cancer treatment.

I am a Master's student in the Department of Chemistry at the University of Colorado Denver, where I am working under the supervision of Prof. Woonghee Lee. My research focuses on creating software programs for analyzing biomolecular NMR, and I am excited about the potential of this work to make important contributions to the field. Outside of my studies, I have a passion for a few other things. I love trying new food, growing plants, and taking pictures. These hobbies help me to stay balanced and remind me of the importance of taking breaks and enjoying the small things in life.

My area of research is centered on the development of software programs that facilitate the analysis of biomolecular NMR. Our laboratory has designed an innovative suite of software programs, known as the POKY suite, which offers automated and visually-enhanced platforms for various essential tasks, such as resonance assignments, structure calculation, dynamics studies, and computer-aided drug design. My particular focus is on developing advanced NMR data analysis tools that can aid in computational analysis of biomolecules. Specifically, my goal is to create next-level tools that can help researchers better understand the structure, function, and interactions of biomolecules at the molecular level. This work involves developing new algorithms, improving existing tools, and combining multiple techniques to create more powerful and efficient analysis methods. Ultimately, my research has the potential to drive progress in the field of biomolecular NMR analysis, helping to advance our understanding of these complex molecules and the role they play in biological systems.

‍