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Vincent J. Hilser
University of Texas Medical Branch - GalvestonDepartment: Human Biological Chemistry & GeneticsAddress: 5.104 Medical Research Bldg. Galveston, Texas 77555-1068 Phone: (409) 747-6813 Fax: (409) 747.6816 Email: vjhilser@utmb.edu Web: www.hbcg.utmb.edu/hilser/index.htm |
Education
B.S., Chemistry, St. John's University
M.S., Biotechnology, Manhattan College
Ph.D., Biochemistry, Johns Hopkins University
Post-Doctoral Fellow, Johns Hopkins University
Honors
2005 Michael and Kate B�r�ny Young Investigator Award, Biophysical Society
2002 Educator Award for Human Biological Chemistry and Genetics, University of Texas Medical Branch
1999 CAREER Award, National Science Foundation
1997 Finn Wold Young Faculty Travel Award, Protein Society
1996 Finn Wold Post Doctoral Travel Award, Protein Society
1995 Post-Doctoral Fellowship, Monsanto Corporation
1991 Excellence in Research Award, Sigma Xi Honor Society - Manhattan College Chapter
Research Topic
Experimental and theoretical studies of protein structure and dynamics.
Research Description
Research in our lab is focused on the experimental characterization of conformational fluctuations, the development and refinement of a general ensemble-based model for fluctuations, and the projection of this thermodynamic model into genomic analysis. Our goals are to unify the description of protein behaviors in such a way as to understand their relationships at the phenomenological level, to codify these relationships in a simple structure-based model, and to apply our model to a number of experimental systems that can be used to test and refine our approach.
Current research projects in the lab focus on four areas. First, we are using calorimetry, hydrogen exchange and NMR relaxation to investigate the role of dynamics in binding for two model systems, the C-terminal SH3 domain of SEM5 and dihydrofolate reductase. Second, we are monitoring the binding of SEM5 SH3 domain to the Sos peptide using titration calorimetry and NMR in order to investigate the conformational bias of unfolded proteins and peptides for the polyproline II conformation. Third, we are using our unique ensemble-based computational approach, COREX/BEST, to investigate the physical basis of energy propagation and signal transduction in proteins. Fourth, we are developing a protein fold classification scheme that is based on a thermodynamic rather than a structural description of proteins.
Selected Publications
- Pan, H., Lee, J.C. and Hilser, V.J. (2000). Binding Sites in Escherichia Coli Communicate by Modulating the Conformational Ensemble. Proc. Natl. Acad. Sci. USA 97: 12020-12025.
- Babu, C.R., Hilser, V.J. and Wand, A. J. (2004). Direct Access to the Cooperative Substructures of Proteins and the Protein Ensemble via Cold Denaturation. Nat. Struct. Mol. Biol. 11: 352-357.
- Ferreon, J.C., Hamburger, J.B. and Hilser, V.J. (2004). An Experimental Strategy to Evaluate the Thermodynamic Stability of Highly Dynamic Binding Sites in Proteins Using Hydrogen Exchange. J. Am. Chem. Soc. 126: 12774-12775.
- Hamburger, J.B. Ferreon, J.C., Whitten, S.T. and Hilser, V.J. (2004). Thermodynamic Origins and Consequences of the Polyproline II (PII) Conformational Bias in the Denatured States of Proteins. Biochemistry. 43: 9790-9799.
- Whitten, S.T., Garcia-Moreno E.B., and Hilser, V.J. (2005). Local Fluctuations Can Modulate the Coupling Between Proton Binding and Global Structural Transitions in Proteins. Proc. Nat. Acad. Sci. USA. 102: 4282-4287.
- Liu, T., Whitten, S.T., and V.J. Hilser (2007) Functional Residues Serve a Dominant Role in Mediating Cooperativity of the Protein Ensemble Proc. Nat. Acad. Sci. USA. In Press.
- Hilser, V. J. and E. B. Thompson (2007) Intrinsic Disorder as a Mechanism to Optimize Allosteric Coupling in Proteins. Proc. Nat. Acad. Sci. USA. In Press.
Lab Members
Lab Photos
Last edited on: September 21, 2009