A Statistical Thermodynamic Model of the Protein Ensemble

Vincent J. Hilser has earned a B.S. degree in chemistry from St. John's University (1987), an M.S. degree in biotechnology from Manhattan College (1991), and a Ph.D. in biochemistry from The Johns Hopkins University (1995). From 1995 through 1997, he did postdoctoral research in the lab of Ernesto Freire (John Hopkins University). In 1997, he accepted an assistant professor's position at the University of Texas Medical Branch, where currently he is Director of the Sealy Center for Structural Biology and Molecular Biophysics. Research in his lab is directed toward elucidating the physical and energetic basis, as well as the functional consequences, of conformational heterogeneity in proteins and applying this information to the development of novel fold classification schemes and protein design strategies.

Bertrand García-Moreno was born and raised in Mexico City. He earned an A.B. degree in biochemistry from Bowdoin College and a Ph.D. in chemistry under the direction of Prof. Frank Gurd at Indiana University in Bloomington. He did postdoctoral research with Prof. Gary Ackers at Johns Hopkins University and at Washington University School of Medicine in St. Louis. He returned to Johns Hopkins in 1992 to join the Department of Biophysics. Research in his laboratory is currently focused on experimental and computation studies of structure-energy relationships and electrostatic effects in proteins.  

Terry Oas received a Ph.D. from the University of Oregon in 1986. Currently, he is an Associate Professor of Biochemistry and Chemistry at Duke University. His lab is primarily interested in the mechanisms of protein folding.

Greg Kapp finished his undergraduate degree in biology and chemistry at the University of Richmond in 1997. He continued his education at the Duke University Medical Center where he pursued his Ph.D. with Terry Oas in the Department of Biochemistry. Greg's Ph.D. project focused on experimental and theoretical investigation of the kinetics of protein folding. Greg's experimental work involved investigation of individual sites in the model protein monomeric λ repressor and how sequence changes in these positions affect the kinetics of protein folding and unfolding. In his theoretical work, Greg concentrated on implementing microscopic reversibility and modeling of substrate unfolding rates in the diffusion−collision model for protein folding. Greg received his Ph.D. in 2003 and is now a postdoctoral fellow in Tanja Kortemme's laboratory in the Department of Biopharmaceutical Sciences at the University of California, San Francisco. Greg is currently computationally and experimentally redesigning protein and protein−protein interactions involved in cellular signaling events.  

Steven Whitten received a B.S. degree (Physics) in 1994 from the University of Nebraska at Omaha and a Ph.D. from the Department of Biophysics at The Johns Hopkins University in 1999. Under the guidance of Prof. Bertrand García-Moreno, his Ph.D. thesis centered on experimental dissection of the residue-specific contributions to pH-dependent stability in staphylococcal nuclease. Following a postdoctoral fellowship in 2000 in the labs of Profs. Michael Blaber and Timothy Logan (Florida State University), he has since worked as a research scientist in the lab of Prof. Vincent Hilser at the University of Texas Medical Branch. There, his primary interest has been in developing computational models of the solution-dependent behavior of protein structure with a particular focus on pH, temperature, salt, and osmolyte effects.