. "APPENDIX D COMMITTEE ON PROPOSAL EVALUATION FOR ALLOCATION OF SUPERCOMPUTING TIME FOR THE STUDY OF MOLECULAR DYNAMICS." Report of the Committee on Proposal Evaluation for Allocation of Supercomputing Time for the Study of Molecular Dynamics. Washington, DC: The National Academies Press, 2010.
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Report of the Committee on Proposal Evaluation for Allocation of Supercomputing Time for the Study of Molecular Dynamics
used to study the mechanism of action of antiviral compounds, and the molecular mechanism for phosphotyrosine control of protein function in signal transduction.
Klaus Schulten received his Ph.D. from Harvard University in 1974. He is Swanlund Professor of Physics and is also affiliated with the Department of Chemistry as well as with the Center for Biophysics and Computational Biology at the University of Illinois, Urbana-Champaign. Professor Schulten is a full-time faculty member in the Beckman Institute and directs the Theoretical and Computational Biophysics Group. His professional interests are theoretical physics and theoretical biology. His current research focuses on the structure and function of supramolecular systems in the living cell, and on the development of non-equilibrium statistical mechanical descriptions and efficient computing tools for structural biology.
Jeffrey Skolnick received his B.A. in Chemistry, Summa Cum Laude, from Washington University, St. Louis in 1975. He received his M. Phil. in Chemistry from Yale University in 1977 and his Ph.D. in Chemistry from Yale University in 1978, with Professor Marshall Fixman. Dr. Skolnick is a Professor at Georgia Technical University and Director of the Center for the Study of Systems Biology. Dr. Skolnick has recently completed a very promising study in cancer metabolomics where he and his research group validated a predictive algorithm that can identify novel metabolites with anticancer properties. They have also developed a new, powerful algorithm that can predict protein function and binding sites, and which can be used for rapid screening ligand libraries. In addition, Dr. Skolnick has developed physics based, atomic potentials for protein structure refinement. He and his team demonstrated that the library of all protein folds is above the percolation threshhold, i.e., any protein structure can be related to any other by no more than eight intermediate structures.
Feng Wang received his B.S. in Chemistry from Peking University (1998) and Ph.D. in Theoretical Chemistry from the University of Pittsburgh (2003). He did post-doctoral research in computational physical chemistry at the University of Utah with Professor Gregory A. Voth. Since 2005, he has been an Assistant Professor in the Department of Chemistry at Boston University. Dr. Wang received a Mellon Fellowship at the University of Pittsburgh in 2002, an NSF CAREER Award in 2007, and an HP Outstanding Junior Faculty award in 2010. His research focuses on systematic development of high quality force fields, free energy determinations, and enhanced sampling.
Arieh Warshel received his BS degree in Chemistry, Summa Cum Laude, from Technion Israel in 1966, and his MS and PhD degrees in Chemical Physics in 1967 and 1969, respectively, from the Weizmann Institute of Science, Israel. After his PhD, he did postdoctoral work at Harvard University. From 1972 to 1976, he was at the Weizmann Institute and at the MRC Laboratory for Molecular Biology in Cambridge, England. In 1976 he joined the faculty of the Department of Chemistry at USC, where he now is Professor of Chemistry and Biochemistry. and a Full Member of the USC Norris Cancer Center. Dr. Warshel has authored over 350 peer-reviewed research articles (H index 92) and book chapters, two books, and several key computer programs. Dr. Warshel’s research focuses on simulations of the functions of biological system and other challenging problems in modern computational biophysics and chemistry. He and his coworkers have pioneered the key approaches for simulating the functions of biological molecules, including introducing molecular dynamics (MD) in Biology, developing the quantum mechanical/molecular-mechanical (QM/MM) approach, introducing simulations of enzymatic reactions, developing simulations of electron transfer and proton transfer processes in proteins, pioneering microscopic modeling of electrostatic effects in macromolecules and introducing simulation of protein folding. Dr. Warshel received the Tolman Medal in 2003, has been elected a Fellow of the Biophysical Society in 2000, a Fellow of the Royal Society of Chemistry in 2008, and a Member of the National Academy of Science in 2009.