Professor Sharp is a world renowned and internationally recognized expert in HRPF. He has published more than 25 peer-reviewed articles in the field of HRPF method development, fundamentals, and applications between 2002 and today, with over forty-five publications overall. Professor Sharp published the first benchtop methods for HRPF, including the first method using UV photolysis of hydrogen peroxide for hydroxyl radical generation.

With numerous invited lectures to both academia and private industry on the application of HRPF to biotherapeutics, Dr. Sharp has addressed problems associated with formulation, biosimilarity, aggregation, and protein-protein and protein-ligand interaction mapping. Professor Sharp’s lab is also known for their work in glycosaminoglycan structure-function analysis, and his team commonly leverages their expertise in both areas to study protein-carbohydrate complexes.

Professor Sharp received his PhD in 2003 from a joint program between Oak Ridge National Laboratory and the University of Tennessee, under the mentorship of Dr. Robert Hettich. He performed his postdoctoral studies at the National Institute of Environmental Health Sciences in the Laboratory of Structural Biology, under the supervision of Dr. Kenneth Tomer. In 2007, he joined the University of Georgia’s Complex Carbohydrate Research Center as a research faculty member. Most recently, Professor Sharp joined the faculty at the University of Mississippi School of Pharmacy, where he currently serves as an Associate Professor of Pharmacology, Associate Professor of Chemistry and Biochemistry, and Director of the Glycoscience Center of Research Excellence.

He has received multiple awards for excellence in research, most recently winning the New Investigator Research Award from the University of Mississippi School of Pharmacy and being designated the University of Mississippi nominee for the 2019 Blavatnik Award in Life Sciences. Professor Sharp serves on multiple national and international advisory and review panels as an expert on protein and carbohydrate biophysical and structural analysis by mass spectrometry.

Professor Orlando has more than 40 years of experience with mass spectrometry, over 30 of these years focused on the identification/characterization of proteins and their post-translational modifications with MS. He currently directs the mass spectrometry research laboratory at the Complex Carbohydrate Research Center (CCRC).

Dr. Orlando has co-authored over 150 publications in peer-reviewed journals, given over 100 invited lectures at various conferences, and served on over 45 NIH review panels. Ron has won numerous awards including being named a NATO Advanced Study Fellow, a Leader of Tomorrow by Spectroscopy magazine, and has won the Outstanding Association of Biomolecular Resource Facilities (ABRF) Presentation Award twice. He has organized and taught short courses on the Analysis of Glycoproteins by Mass Spectrometry at meetings of the American Society for Mass Spectrometry (ASMS) and International Symposium and Exhibit on the Separation of Proteins, Peptides & Polynucleotides (ISPPP). Professor Orlando is the founder and past chair of the ABRF Glycoprotein Research Group and is frequently invited to give lectures on his mass spectrometry-based research. Further, Professor Orlando is the Editor-in-Chief of the Journal of Biomolecular Techniques.

Professor Orlando has firsthand experience with small start-up companies, having founded three spin-off/start-up companies: BioInquire in 2007, GlycoScientific in 2009, and PhotoChem Technologies in 2012. BioInquire became profitable in 2008, and in 2010 it was acquired by NuSep (a publicly-traded, Australian company). Professor Orlando was given the award of Entrepreneur of the Year from the Georgia BioBusiness Center because of his critical role in BioInquire’s success. Moreover, he has also been nominated to be a Senior Member of the National Academy of Inventors by Innovation Gateway.

Professor Chance is an internationally recognized expert in proteomics and structural biology who has built multiple science and training programs over a 30-year career in academia. He has published over 300 papers with over 15,000 citations. He is currently Vice Dean for Research and holds the titles of Distinguished University Professor, the Charles W. and Iona A. Mathias Professor of Cancer Research, as well as Professor appointments in the Departments of Nutrition, Genetics & Genome Sciences, and General Medical Sciences at the School of Medicine of Case Western Reserve University (CWRU). He is the founding director (since 2005) of the Center for Proteomics and Bioinformatics and founding director of the Center for Synchrotron Biosciences (since 1994). Prior to his appointment at CWRU, Dr. Chance was professor of Physiology and Biophysics at Albert Einstein College of Medicine.

At Einstein, Dr. Chance developed a synchrotron-based radiolysis and “footprinting” approach to define the folding mechanism of the Tetrahymena ribozyme on millisecond timescales, revealing fundamental principles of RNA packing. Subsequently, Dr. Chance envisioned an approach to develop protein structure assessment using OH-radical footprinting technology.

With the demonstration of mass spectrometry (MS) detection of OH-radical modifications in peptides in a landmark paper in Analytical Chemistry (1999), the field of Hydroxyl Radical Protein Footprinting (HRPF) was born.

Professor Michael Gross originated the process of Fast Photo-oxidation of Proteins (FPOP) Hydroxyl Radical Protein Footprinting (HRPF).

At Washington University in St. Louis, the Gross research group focuses mainly on the development of mass spectrometry (MS) in biophysics and structural proteomics, specifically to probe protein-ligand interaction interfaces, affinities, aggregation, and folding/unfolding. The work includes both instrument and method development and application to important proteins and protein complexes. His research group also employs specific chemical reagents to footprint proteins and determines their interfaces and orientations in complex biological settings, hydrogen/deuterium exchange, and native MS.

Professor Gross received his PhD at the University of Minnesota under the tutelage of E.A. Hill and was a postdoctoral person with E.R. Thornton at U of Penn and then with F.W. McLafferty at Purdue. He began his independent career in 1968 as Assistant Professor at the University of Nebraska-Lincoln where he directed an NSF Center for Mass Spectrometry. In 1994, he joined Washington University in St. Louis and assumed the role of PI of an NIH Research Resource in Mass Spectrometry.

Professor Gross is a highly cited chemist who has won the American Chemical Society Field and Franklin Award, the ACS Midwest Award, and the ACS Analytical Chemistry Award. He was awarded the JJ Thomson Medal and the Eastern Analytical Symposium Award for Distinguished Contributions to Mass Spectrometry and the Commonwealth of Massachusetts Pioneer Award for “In Search of the Health Consequences of Dioxin in Our Environment.” He was honored by the Washington University Graduate Student Senate with the Outstanding Mentor Award in 2001. He is founding editor of the Journal of the American Society for Mass Spectrometry, coeditor of the Encyclopedia of Mass Spectrometry (published by Elsevier), and was editor until 1990 of Mass Spectrometry Reviews. He has served on numerous editorial boards and as a consultant to industry and academic laboratories.

Professor Lisa Jones has pioneered the field of in-cell and whole-organism FPOP. In the Department of Chemistry and Biochemistry at UCSD, the Jones Lab is a structural proteomics group that uses biochemical, analytical, and biophysical approaches to study protein interactions important in biological processes. Their research focuses on using protein footprinting methods coupled with mass spectrometry to identify these interactions. A major focus of their lab is extending FPOP as an in-cell method for monitoring proteins in their native cellular environment. This method would be especially useful for membrane proteins, the largest class of drug targets, which are challenging to study in vitro owing to the difficulty of purifying these proteins. The Jones lab has further expanded FPOP for in vivo analysis in C. elegans, an animal model for human disease.

Dr. Jones received her PhD at Georgia State University studying the affinity effectors of calcium binding proteins. She was a postdoctoral associate in the lab of Dr. Peter Prevelige at the University of Alabama-Birmingham where she used hydrogen deuterium exchange mass spectrometry to study protein interactions in virus capsids. Dr. Jones was a postdoctoral associate in the lab of Dr. Michael Gross at Washington University in St. Louis where she expanded the use of the FPOP method for studying biologics.

Since completing his PhD in 2003, Professor Tabb has invested considerable effort in proteomics technology assessment, bioinformatics, and biostatistics education, quality control for mass spectrometry, and non-model organism biology.

He has authored approximately 140 peer-reviewed articles and book chapters.  Since 2015, Prof. Tabb has become a globetrotter, first spending five years in South Africa at Stellenbosch University and currently spending two years in France.

A key principle that has animated Prof. Tabb’s career is the conviction that researchers must understand the fundamental algorithms of the software they use for their research data.  The algorithms that proteomics researchers use to identify tandem mass spectra to peptide and proteoform sequences are the most common topic for his teaching.  During 2022, he will teach short courses on this subject for the American Society of Mass Spectrometry conference, the International Mass Spectrometry Conference, and the Human Proteomics Organization World Congress.

With a strong background in detecting post-translational modifications and a fascination with protein structure models, Prof. Tabb is excited about the possibilities of HRPF. His experience of proteogenomics has sought to understand the perturbation of protein structures resulting from replacing one amino acid with another.  HRPF is a promising lens to examine structure via mass spectrometry.