Virgil L. Woods, Jr.
Professor of Medicine
M.D., University of California, San Francisco
Chair, BMS Research Proposition Qualifying Exam
Director, UCSD DXMS Proteomics Resource
Our efforts are focused on structural biology applications of an advanced proteomics technology developed at UC San Diego, enhanced hydrogen/deuterium exchange mass spectrometry (DXMS). Our goal is to provide DXMS as a readily accessible tool for collaborating investigators interested in applying it to important issues in protein structure and dynamics. It can be used to rapidly determine the high-resolution structural dynamics of proteins, alone or in combination with other proteins, DNA, or small-molecule ligands. A typical study can be completed in 2-4 months employing a few hundred micrograms of the study protein. Collaborators provide the study protein and experimental questions, and design the experiments with us. We then perform most aspects of the DXMS data acquisition, and interpret the results in concert with the collaborator.
Trainees first rotate through our DXMS resource where they learn the theory and practice of DXMS while acquiring and processing data on their study proteins. When they return to their parent labs, the trainees are fully able to continue the same or additional DXMS studies with us remotely. Some collaborators have subsequently set up their own DXMS instrumentation with our guidance. Students who rotate through our lab leave with cutting-edge expertise in DXMS analysis that is readily applicable to any protein of interest to them.
On the basis of an unprecedented perfect (10.0) Study Section priority score, were recently awarded a highly competitive $1M High-End NIH instrumentation grant to outfit the Woods lab with the world's most advanced mass spectrometers and associated robotics for our future DXMS studies.
Proteomics, mass spectrometry, protein structure, structural biology, crystallography, allostery, conformational change, chemical biology, biochemistry, molecular biology, chemistry, enzyme, cancer therapeutics, molecular pharmacology, hydrogen exchange, H-D exchange, HXMS, DXMS
BMS Focus Areas:
Structural Chemical Biology
Chen, H., D. Ricklin, M. Hammel, B.L. Garcia, W.J. McWhorter, G. Sfyroera, Y.Q. Wu, A. Tzekou, S. Li, B.V. Geisbrecht, V.L. Woods, Jr., and J.D. Lambris. 2010. Allosteric inhibition of complement function by a staphylococcal immune evasion protein. Proc Natl Acad Sci U S A 107:17621-17626.
Damo, S.M., A.H. Phillips, A.L. Young, S. Li, V.L. Woods, Jr., and D.E. Wemmer. 2010. Probing the conformation of a prion protein fibril with hydrogen exchange. J Biol Chem 285:32303-32311.
Li, S., T. Tsalkova, M.A. White, F.C. Mei, T. Liu, D. Wang, V.L. Woods, Jr., and X. Cheng. 2011. Mechanism of intracellular cAMP sensor Epac2 activation: cAMP-induced conformational changes identified by amide hydrogen/deuterium exchange mass spectrometry (DXMS). J Biol Chem 286:17889-17897.
Chung, K.Y., S. Rasmussen, T. Liu, S. Li, B.T. DeVree, P. Seok, D. Calinski, B.K. Kobilka, V.L. Woods Jr., and R.K. Sunahara. 2011 b2 adrenergic receptor-induced conformational changes in the heterotrimeric G protein Gs. Nature, In Press.