At this two-day event, you will experience a variety of presentations from top-ranked scientists on thewide-ranging applications of stable isotopes. These include MS and NMR facilitated research in environmental analysis, metabolism, metabolomics, proteomics, protein structure determination, RNA/DNA studies, and more!

On Demand Recordings, Transcriptions, Presentation Titles, Abstracts, and Speaker Biographies

Guidelines, Considerations, and Benefits of Incorporating QCs into MS ‘Omics Experimental Practices

UllasAndrew Percy, PhD | MS 'Omics Product Manager
Cambridge Isotope Laboratories, Inc. (USA)

Abstract: Mass spectrometry (MS)-based methods can return degrees of variability that impacts the rigor and reproducibility of the acquired results.  To help monitor this potential issue, quality control (QC) measures must be entrenched in experimental designs and analytical workflows.  The type and placement of QC samples in a batch sequence are important considerations to the assessment process.  Here, we describe a systematic approach to designing a MS-based QC workflow utilizing different types of QC samples (with and without isotopically labeled QReSS standards) positioned around a metabolomics study application.  The guidelines and lessons gleaned will be presented along with insights into the significance of QCs in MS ‘omics studies. 

During this webinar, you will learn about: 

  • QC is an integral aspect of experimental design. 
  • Types and order of QC samples play a role in assessing method and instrument performance. 
  • Case examples of QCs impact on MS ‘omics workflows. 
On Demand Recording


Biography: Dr. Andrew Percy received his MSc and PhD in Analytical Chemistry from the University of Calgary (Canada).  In 2011, he joined the UVic-Genome BC Proteomics Centre (Victoria, Canada) as a post-doctoral fellow and served as the Quantitative Proteomics group leader from 2012 on.  He has been at Cambridge Isotope Laboratories, Inc. (CIL) since 2016 as a Senior Applications Chemist for Mass Spectrometry and relatively recently as the MS ‘Omics Product Manager.  Dr. Percy’s role at CIL capitalizes on his deep R&D background in MS ‘omics where he utilized stable isotope-labeled materials in different ways to qualify/quantify analytes in various types of biosamples.  Included is his involvement in the development/application of ‘omics-related products, such as quality control and quantification mixes.  To date, Dr. Percy has co-authored more than 50 articles (~50% primary) in MS 'omics, is an active member of the Metabolomics Quality Assurance & Quality Control Consortium, and is a routine reviewer of ‘omics manuscript submissions across several scientific journals. 

Heavy Isotopes for Discovery and Clinical Assay Development

HeatherAkhilesh Pandey, MD, PhD | Professor
Mayo Clinic (USA)

Abstract: In-depth coverage of highly complex protein mixtures such as plasma, cell and tissue proteomes, in discovery studies has become routine because of advances in liquid chromatography and mass spectrometry instrumentation. However, accurate quantitation of proteins requires targeted approaches such multiple or parallel reaction monitoring (MRM/PRM) and the use of heavy isotope labeled versions of peptides/proteins. I will describe how we have used isotopically labeled standards including the SISCAPA (stable isotope standards and capture with anti-peptide antibody) approach in our studies to develop mass spectrometry-based assays for SARS-CoV-2 viral antigens, variant peptides and host response proteins. Finally, I will also discuss development of novel assays involving triggered acquisition based on heavy spiked-in peptides using the SureQuant approach.

During this webinar, you will learn about:

  • Targeted analysis for highly sensitive detection of viral antigens.
  • Use of SISCAPA approach involving anti-peptide antibodies.
  • SureQuant method for developing highly sensitive quantitative assays.

Recording is unavailable

Biography: Dr. Akhilesh Pandey is currently a Professor in the Department of Laboratory Medicine and Pathology and the Center for Individualized Medicine at Mayo Clinic in Rochester, Minnesota. He has pioneered methods for quantitative proteomics (SILAC), for analysis of post-translational modifications, protein-protein interactions and proteogenomics analyses. Dr. Pandey’s laboratory is taking a systems biology approach by combining many 'Omics' technologies to study signal transduction pathways in health and disease. He is also developing a variety of novel mass spectrometry-based assays for use as diagnostics in clinical settings.

The Discovery of Novel PFAS in Environmental Samples Using High Resolution Mass Spectrometry 

HeatherMark Strynar, PhD | Physical Scientist 
Office of Research and Development of the U.S. Environmental Protection Agency (USA)

Abstract: Targeted analysis methods for chemicals in environmental media are the backbone of monitoring studies. These methods are highly multi-laboratory validated and time-tested approaches for a host of environmental studies. However, there are shortcomings to this approach. The chosen methods only monitor for a select set of analytes. High-resolution mass spectrometry (HRMS) instrumentation (such as quadrupole time of flight and orbital ion trap systems) partially fills this void by allowing the analysis of chemicals without any preconceived notion of what is in the sample being analyzed. This is done through two main approaches: 1) suspect screening—screening for chemicals in a large list, or 2) non-targeted screening—true novel compound discovery and structure elucidation. This approach is not without its own deficiencies as well. The selected extraction techniques and instrument used (such as GC vs LC) bias the possible detected analytes and is not comprehensive. Additional challenges include generally more expensive instrumentation, more laborious data processing and mining techniques, extremely large data sets, and often a lack of chemical standards for compound confirmation and quantitation. An added benefit of HRMS analysis is that data of previously run samples can be mined in future efforts to explore chemicals that were either unknown at the time of analysis or were overlooked. Non-targeted methods should inform analysts about what chemicals should be added to targeted analysis methods, not take the place of them. This talk will present approaches used in the discovery of xenobiotic PFAS chemicals in environmental media using HRMS application. 

During this webinar, you will learn about:

  • PFAS are very different from many other organic compounds.  
  • Discovery of new PFAS is the basis for additional work needing to be done. 
  • HRMS is a key tool in this discovery effort. 
On Demand Recording


Biography: Mark Strynar is a Physical Scientist in the Office of Research and Development of the U.S, Environmental Protection Agency since 2002. His research interests include the use of high resolution mass spectrometry (HRMS) to investigate the fate and transport of per and poly fluorinated compounds (PFAS) and other xenobiotic compounds in biological and environmental media.  Additionally, he is interested in novel compound discovery in environmental media and development of analytical methods for unique biomarkers of exposure to chemicals that are useful for dosed animal or human epidemiological studies.

A Targeted Metabolomics Approach for Quantifying a Broad Constellation of Bile Acids in Biomedical Research 

UllasAmy Engevik, PhD | Assistant Professor
The Medical University of South Carolina (USA)

Abstract: Bile is a liver-produced secretion that is stored in the gallbladder. Bile contains a broad constellation of bile acids (BAs). The liver synthesizes primary BAs that can be further modified by intestinal microbes to form secondary BAs that can exist in non-conjugated, and amino acid conjugated forms. The amphipathic properties of BAs aid in emulsification of ingested food, absorption of fat-soluble vitamins, and digestion of dietary lipids in the gut. BAs also serve as signaling compounds by which host and intestinal microbes communicate along the gut-liver-axis. Due to the physicochemical properties of bile acids/salts (i.e., hydrophobic and ionizable), the application of reverse-phase liquid chromatography-tandem mass spectrometry (LC-MS/MS)-based methods are ideally suited for the measurement of these compounds in a number of biofluids and tissues often surveyed in biomedical research. Recently, the molecular motor Myosin Vb has been implicated in a variety of cholestatic liver disorders that arise from an inability to properly secrete bile acids. In this presentation we will present our findings of altered bile acid concentrations and changes in proteins in the liver and ileum of mice lacking the molecular motor Myosin Vb.

During this webinar, you will learn about: 

  • A scheduled Multiple Reaction Monitoring (sMRM) scan mode is used to monitor quantifying and qualifying transitions for each of 16 bile acids (BAs) and their corresponding deuterated internal standard analog. 
  • The chromatographic method is capable of resolving all BAs with isobaric precursor-to-product ion transitions. 
  • The method has been adapted to measuring the bile acid levels in homogenized liver and ileum tissues, homogenized feces, and plasma or serum samples. 
On Demand Recording


Biography: Dr. Amy Engevik received her PhD from the University of Cincinnati and joined the MUSC faculty in 2021 as an Assistant Professor following postdoctoral work studying gut epithelial biology and the basic mechanisms underlying enteric disease in the Department of Surgery at the Vanderbilt University Medical Center. Dr. Engevik’s laboratory focuses on understanding how myosin motors function in the gastrointestinal tract under homeostatic conditions and in disease states. Amy uses animal models, human tissue samples and organoid cultures to elucidate the role of Myosin Vb in congenital diarrheal disorders, liver cholestasis and various cancers. Amy’s expertise in immunofluorescence staining and imaging has resulted in a number of publications that report how Myosin Vb regulates apical trafficking patterns in the intestine. Amy’s research group is currently developing novel mouse models lacking functional Myosin Vb to investigate how Myosin Vb regulates bile acid secretion and bile acid signaling in the intestine and liver. 

Use of 13C- Labeled Internal Standards for Accurate Determination of 6PPD Quinone

UllasAndrew Patterson | Technical Director
Eurofins Environment Testing America (USA)


During this webinar, you will learn about: 

  • Environmental chemistry would not be what it is today without isotopically labeled analogues.
  • There is so much focus on LOQ and without isotope dilution, these data would not hold the same confidence.
  • There will always be the "next" dioxin or PFAS or emerging contaminant.
On Demand Recording


Biography: Andrew is the Corporate Technical Director for Eurofins Environment Testing America for the Specialty Services division.  He brings over 20 years of experience in the environmental laboratory industry with a focus on HRGC/HRMS analyses and also LC-MS/MS analyses. These approaches have focused on PCBs, Dioxins, brominated flame-retardants, PFAS, emerging contaminants and human biomonitoring. He is among a handful of Eurofins scientists focused on advanced analytical techniques such as Non-target Analysis (NTA) via LC-QToF instrumentation. Prior to Eurofins, Andrew was the Technical Director for an analytical laboratory in Northern California where he developed PFAS and PPCP (Pharmaceuticals and personal care products) capability within the lab and oversaw HRMS operations. Andrew holds a Bachelor’s of Science in Microbiology with a concentration in Biochemistry from Cal Poly San Luis Obispo, California, USA.

Post-prandial Protein Handling: ‘You are What you Eat’ 

UllasLuc van Loon, PhD | Professor
Maastricht University (The Netherlands)

Abstract: Skeletal muscle protein is constantly being synthesized and broken down, with a turnover rate of about 1-2% per day. The rate of skeletal muscle protein synthesis is regulated by two main metabolic stimuli, food intake and physical activity. Using stable isotope labeled amino acid tracers and/or the use of specifically produced, intrinsically labeled protein we can study post-prandial protein handling and muscle protein synthesis rates in vivo in humans. Ingestion of a single meal-like amount of protein allows ~55% of the protein derived amino acids to become available in the circulation, with approximately 20% of the protein derived plasma amino acids taken up in skeletal muscle tissue during a 5 h post-prandial period, thereby stimulating muscle protein synthesis rates and providing precursors for de novo muscle protein. In conclusion ‘you are what you just ate’. 

During this webinar, you will learn about: 

  • Labeled amino acid tracers are instrumental in understanding the kinetics of post-prandial protein handling in vivo in humans. 
  • Protein digestion and amino acid absorption define the capacity for post-prandial stimulation of muscle protein synthesis. 
  • You are what you just ate. 

Recording is unavailable

Biography: Professor van Loon was appointed Professor of Nutrition and Exercise at Maastricht University in The Netherlands in 2010. He also serves as a visiting Professor at the Free University of Brussels in Belgium and the Australian Catholic University in Melbourne, Australia. Luc has an international research standing in the area of skeletal muscle metabolism, has published well over 400 peer-reviewed articles (more than 20.000 citations) achieving an H-index of 80. Current research in his laboratory focuses on the skeletal muscle adaptive response to physical (in)activity, and the impact of nutritional and pharmacological interventions to modulate metabolism in both health and disease. The latter are investigated on a whole-body, tissue, and cellular level, with skeletal muscle as the main tissue of interest. He is active in various media to translate research findings to the general public, highlighting the impact of nutrition and physical activity to support performance and health. To support the use of stable isotopes in biomedical research, he is also scientific coordinator of the Stable Isotope Research Centre (SIRC) at Maastricht University Medical Centre.

The Role of Long-Lived Proteins in Health and Neurodegeneration

UllasJeffery Savas, PhD | Assistant Professor
Northwestern University, Feinberg School of Medicine (USA)

Abstract: I will describe our recent discovery of intracellular long-lived proteins using metabolic pulse-chase labeling of rodents and proteomic analysis. First, I will summarize our finding that a subset of the mitochondrial proteome unexpectedly persists for months selectively in tissues enriched with long-lived post-mitotic cells. Second, I will describe how we used a similar strategy to identify synaptic vesicle associated proteins with impaired degradation during the onset of amyloid pathology in mouse models of Alzheimer’s disease and how this has advanced our understanding. 

During this webinar, you will learn about: 

  • Protein turnover can be studied in vivo using stable isotope metabolic labeling with mass spectrometry-based proteomics. 
  • Stable isotopic labeling can be coupled to chemical crosslinking and multiplexed analysis. 
  • The identification of long-lived proteins accelerates biological discovery. 
On Demand Recording


Biography: Jeffrey Savas received a B.S. in Biochemistry at the University of California, Santa Cruz. He obtained his PhD from New York University School of Medicine and performed postdoctoral training at The Scripps Research Institute. The goal of his research is to determine how impaired protein quality control contributes to synaptic dysfunction and aging. The lab is currently working to: (1) develop new tools to anatomize specific synaptic proteomes, (2) investigate cochlear proteostasis and, (3) identify proteins with hampered degradation dynamics during neurodegeneration. 

CIL Products for Biomolecular NMR

UllasKelly Andrade | Assistant Product Manager 
Cambridge Isotope Laboratories, Inc. (USA)

Abstract: Nuclear magnetic resonance (NMR) spectroscopy is a valuable tool used to gather information regarding the structure and dynamics of protein and/or nucleic acids at the atomic level. Determination of the three-dimensional structure of these such macromolecules and their complexes is vital for rational drug design and expanding knowledge within the field of mechanistic biology. Here, we briefly describe the benefits and importance of stable isotopes in NMR-based research as well as highlight the common reagents and labeling schemes for enriching protein and nucleic acids for most types of NMR investigations.  Additionally, we will present some new isotopically labeled offerings in this space.

On Demand Recording


Rapid RNA NMR Assignment Process

UllasHarald Schwalbe, PhD | Professor
 Jaohann Wolfgang Goethe-Universität, Institut für Organische Chemie und Chemische Biologie (Germany)

Abstract: In my contribution, I will discuss key lessons learnt in the context of the global Covid19-NMR project. In the context of this project, we assigned 20 RNAs derived from the untranslated parts of SARS-CoV-2. They range in size from 20 - 80 nucleotides (Wacker, Weigand et al., 2020). In this process, we used multiple samples with various labeling pattern. A general pipeline will be discussed. The assignment forms the basis for screening of fragments towards binding of RNA.

During this webinar, you will learn about:

  • Interface between isotope labeling, tailored NMR experiments, rapid assignment and structure determination.
  • 1H and 19F labeling for NMR-based ligand screening.
  • From spectra to information. 
On Demand Recording


Biography: Harald Schwalbe obtained his PhD in Chemistry in 1995 from Goethe University (Frankfurt, Germany) under the supervision of Professor Christian Griesinger. His graduate research was on NMR methods development in protein NMR spectroscopy. He was postdoctoral fellow with Professor Sir Chris Dobson, FRS, at Oxford University (Oxford, U.K.). From 1995 to 1999, he worked on his Habilitation. He accepted an offer to become assistant professor at the Massachusetts Institute for Technology (Cambridge, U.S.A.) in 1999. In 2002, he became full professor of Organic Chemistry at Goethe University. His research focuses on the investigation of structure and dynamics of proteins, DNA, RNA and their complexes, particular with NMR spectroscopy.

Integrative Structural Biology of Protein Assemblies: Challenges and Opportunities for Magnetic Resonance 

UllasTatyana Polenova, PhD  | Professor
University of Delaware (USA)

Abstract: I will discuss recent advances in MAS NMR methods for atomic-resolution structural analysis of large biological assemblies. Using examples of distinct systems studied by our lab, I will illustrate the unique information revealed by MAS NMR about atomic-level 3D structures and drug binding, inaccessible by other techniques. I will demonstrate the power of integrating MAS NMR with medium-resolution cryo-EM and data-driven MD simulations, and discuss the challenges and opportunities for magnetic resonance in integrative structural biology. I will talk about the isotope labeling strategies and needs for NMR-based structural biology.

During this webinar, you will learn about: 

  • MAS NMR provides exquisite atomic-resolution view on structure, dynamics, and ligand large biological assemblies, inaccessible by other means.
  • Integration of NMR and complementary structural biology techniques is a powerful approach for studying large biological assemblies with atomic resolution.
  • Development of new technologies, including isotope labeling strategies, is needed, to take full advantage of unique capabilities of NMR. 

Recording is unavailable

Biography: Tatyana Polenova is Professor of Chemistry and Biochemistry at the University of Delaware. She received her undergraduate degree (diploma with excellence) from Moscow State University in 1992. She received her PhD degree from Columbia University in 1997, working in the laboratory of Professor Ann McDermott. After a postdoctoral position at Columbia, in 1999 she joined the faculty of City University of New York-Hunter College, and in 2003 relocated to the University of Delaware. Her research focuses on solid-state NMR methods development and applications to understanding structure, dynamics and function of biological systems, including viral and cytoskeleton protein assemblies. Polenova is a Fellow of the International Society of Magnetic Resonance. She is the Editor in Chief of Journal of Magnetic Resonance, an Associate Developmental Editor of Journal of Structural Biology and Journal of Structural Biology X, and an Associate Editor of Journal of Biomolecular NMR.

Measuring β-oxidation in the perfused liver with [D15]octanoate

UllasMatthew Merritt, PhD | Associate Professor
University of Florida (USA)

Abstract: Fatty liver disease is commonly associated with disrupted fatty acid oxidation. While experiments measuring hepatic TCA cycle turnover using 13C labeled substrates have produced incongruous results, none of the methods have directly assayed β-oxidation per se. Here we demonstrate that in the perfused mouse liver, a common model of hepatic metabolism, administration of [D15]octanoate results in the production of partially deuterated water (HDO). HDO is produced at multiple steps of β-oxidation and its generation produces a linear correlation with the O2 consumption of the liver. Using Isotopomer Network Compartmental Analysis (INCA), we produce a quantitative model liver metabolism.

During this webinar, you will learn about: 

  • Deuterated water is a product of oxidation of deuterated fatty acids.
  • Magnetic resonance offers a robust means of collecting kinetic data in functioning tissues.
  • β-oxidation is inhibited in mice after 16 weeks of high fat diet.
On Demand Recording


Biography: Matthew Merritt received his PhD in physical chemistry from Washington University in St. Louis in the lab of Dr. Jacob Schaefer. His post-doctoral research focused on DNA structure elucidation with solid state NMR in the lab of Dr. Gary Drobny at the University of Washington. His first academic position was NMR facility manager at UT Southwestern Medical Center working with Dr. Craig Malloy and Dr. Dean Sherry. He ultimately was promoted to Associate Professor before moving to the University of Florida, Department of Biochemistry and Molecular Biology in 2015. His research focuses on developing metabolic imaging methods and applying the technology to models of human disease, including nonalcoholic fatty liver disease.

Examples of Quantitative NMR Analyses in Pharmaceutical Industry 

UllasQiuwei Xu, PhD | Senior Principal Scientist
Merck (USA)

Abstract: This presentation will cover essential components for quantitative NMR analysis, and its application to pharmaceutical R&D.

During this webinar, you will learn about: 

  • Essential components for automated qNMR analysis.
  • Software for metabolite identification and quantification.
  • Areas of qNMR application.
On Demand Recording



Biography: Qiuwei Xu, PhD, is a senior principal scientist in Merck. He leads quantitative NMR operation for metabolomics and vaccine process qualification. The NMR metabolomics lab is automated for quantitative profiling of endogenous metabolites in assisting investigation of drug toxicity or fermentation bioprocess. The endogenous metabolite identification is facilitated by an establishment of NMR reference library of about 800 endogenous metabolites and software for batch processing of metabolite identification and quantification. He published numerous papers in methodology and application of quantitative NMR for metabolomics and vaccine research and development. 

The Power of Isotope Labeling NMR of Proteins

UllasGerhard Wagner, PhD | Professor
Harvard Medical School (USA)

Abstract: The impact of NMR for studies of proteins has skyrocketed from the first recording of a 1D NMR spectrum of ribonuclease in 1957 to NMR structures of proteins, high resolution multiple resonance experiments at high field and structures of large proteins and protein complexes in solution. A key step was introduction of 15N and 13C labeling by bacterial expression in the late 1980s, and the demonstration of the benefits of perdeuteration on spectral resolution, and the impact of methyl TROSY. Over the recent years we focused on a judicious optimizing expression precursors for more efficient backbone assignments, 15N detection, aromatic carbon TROSY and 19F-13C TROSYs. Need for suitable isotope labeled precursors will be presented.

During this webinar, you will learn about:

  • Choice if careful selection of labeled precursors can facilitate assignment of large proteins.
  • 13C 2H labeled precursors can resolve aromatic spectra for protein ligand complexes.
  • 19F TROSY may have great impact in future.
On Demand Recording


Biography: Dr. Gerhard Wagner is the Elkan R. Blout Professor in the Department of Biological Chemistry and Molecular Pharmacology at Harvard Medical School. Wagner obtained his PhD from the ETH Zürich in 1977 with NMR studies of protein dynamics. Subsequently he worked on methods for protein resonance assignment and structure determination. From 1987 to 1990 he was a faculty at the University of Michigan in Ann Arbor where he developed triple-resonance methods for protein assignments. He also developed procedures for studies of protein dynamics. Since 1990 he is Professor of Biological Chemistry and Molecular Pharmacology at Harvard Medical School. His current interests are on eukaryotic translation initiation, transcriptional activation and membrane proteins in micelles and nanodiscs. Current interest is on GPCR signaling mechanisms, and how the receptors signal through G proteins or arrestins.  There is also interest in complexes of the voltage-dependent anion channel, VDAC1, with hexokinases, and the relation to disease. A major effort is on discovery and characterization of small molecule inhibitors of protein-protein interactions.  He is also strongly interested in further development of NMR methods and procedures for advanced sampling and data reconstruction. Dr. Wagner received the Laukien Prize of the ENC, he has been elected to the German National Academy of Sciences (Leopoldina), The National Academy of Science USA and the American Academy of Arts and Sciences

Isotope Labeling in NMR Spectroscopy Based Metabolomics

UllasG.A. Nagana Gowda, PhD | Research Associate Professor
University of Washington (USA)

Abstract: The rapidly growing area of “metabolomics,” in which a large number of metabolites in biological mixtures are analyzed in one step, promises immense potential for numerous areas of basic and applied sciences. Because of its unique ability to detect metabolites in intact biological mixtures as well as live systems in real-time, reproducibly and quantitatively, nuclear magnetic resonance (NMR) spectroscopy has emerged as one of the most powerful analytical techniques in metabolomics. NMR spectroscopy combined with isotope labeling of metabolites has dramatically improved our ability to trace important metabolic pathways as well as quantitatively analyze metabolites. Increased sensitivity and selectivity achieved through isotope labeling have paved novel avenues to unravel biological complexity and gain insights into cellular functions in health and disease conditions. In this presentation, some of the results from ex vivo and in vitro studies made using isotope labeled compounds will be discussed.

During this webinar, you will learn about:

  • Application of isotope labeled compounds for metabolite quantitation. 
  • Increasing sensitivity of metabolite analysis based on isotope tagging of metabolites.  
  • Application of isotope tracers for pathway analysis using ex vivo metabolomics. 
  • Application of isotope tracers for monitoring metabolism in live systems in real time.
On Demand Recording


Biography: G. A. Nagana Gowda is a Research Associate Professor at the Northwest Metabolomics Research Center, Department of Anesthesiology and Pain Medicine, University of Washington, Seattle. From 2006-2012, he was a Research Scientist in the Chemistry Department, Purdue University, West Lafayette, Indiana. Previously, he was an Assistant Professor at the Centre of Biomedical Magnetic Resonance, Lucknow, India. He did his Postdoctoral work at the State University of New York, Buffalo, USA (1996–1998), and worked at the NMR Research Centre, Indian Institute Science, Bangalore, India (1986–2001). He received his BSc degree (Physics, Chemistry, and Mathematics) in 1983 and MSc degree (Analytical Chemistry) in 1985 from Mysore University, India and PhD degree (NMR Spectroscopy) in 1999 from Bangalore University, India. Broadly, his research is in the area of NMR spectroscopy-based metabolomics: methods development and applications focusing mechanistic insights into health and pathophysiology of diseases.

Structure Determination of Large RNAs by NMR

HeatherSarah Keane, PhD | Assistant Professor
University of Michigan (USA)

Abstract: NMR spectroscopy of large RNAs has traditionally been hindered by unfavorable relaxation properties and severe spectral overlap. I will discuss the use of partial deuterium labeling to facilitate resonance assignments and structure determination of large RNAs. 

During this webinar, you will learn about: 

  • 2H incorporation into RNAs.
  • Analysis NOESY-based spectra.
  • RNA structure calculation.

Recording is unavailable

Biography: Sarah Keane graduated from Furman University with a B.S. in Chemistry (2007). Under the direction of David Giedroc, she received a PhD in Chemistry from Indiana University (2012). Sarah then accepted a postdoctoral position with Michael Summers at the Howard Hughes Medical Institute at the University of Maryland Baltimore County. Sarah joined the University of Michigan in January 2017 with a joint appointment in the Biophysics and Chemistry departments. The Keane lab is interested in uncovering the structures and mechanisms of biologically relevant noncoding RNAs using NMR spectroscopy complemented with other biochemical and biophysical tools.