such as protein-ligand binding, solvation, and solubility. His research interests include the binding of small-molecule ligands to proteins and the interactions of small molecules with water and other solvents. Current computational methods have limited accuracy for pharmaceutical drug discovery applications, and his laboratory seeks to develop and apply more accurate methods for computing and even predicting binding affinities. Recent work has also examined solute geometry and the role of entropy in small molecule solvation. Dr. Mobley was previously an Assistant Professor in Chemistry at the University of New Orleans (2008 to 2012) and received the Hewlett-Packard Outstanding Junior Faculty Award in Computational Chemistry from the American Chemical Society (2009). He received his B.S. and Ph.D. degrees in physics from the University of California, Davis.

Richard W. Pastor, Ph.D., is Chief of the Membrane Biophysics Section at the National Heart Lung and Blood Institute of the National Institutes of Health. He received a B.A. in philosophy from Hamilton College (1973), a M.S. in chemistry from Syracuse University (1977), and Ph.D. in Biophysics from Harvard University (1984). He did research and review at the Food and Drug Administration from 1984 to 2007, and moved to the National Institutes of Health in 2007. His research focuses on computer simulations of membranes, including method development (all-atom and coarse grained lipid force fields); fundamental theory (treatment of diffusion in two dimensions, and spontaneous curvature in membranes); biological applications (conformations of peptides in bilayers; fencing of PIP2); and technological applications (polymer transport through ion channels). Dr. Pastor is also a CHARMM developer (algorithms involving pressure anisotropy and long range forces).

Loukas Petridis, Ph.D. is a Research Staff Scientist in the Center for Molecular Biophysics at Oak Ridge National Laboratory. His research focuses on high-performance computer simulation of biological macromolecules, neutron scattering in bioenergy research and polymer physics. In particular, he investigates the origins of biomass recalcitrance via the integration of computer simulation with neutron scattering experiments, undertakes computer simulations of lignocelluloses, and investigates molecular-scale mechanisms stabilizing soil organic carbon by application of molecular dynamics simulation and neutron reflectometry. He also studies scaling of molecular dynamics simulation on supercomputers and physics of biopolymers. He obtained his Ph.D. in theoretical physics from Cambridge University in 2006 and was a postdoctoral fellow at Oak Ridge National Laboratory from 2007 to 2009.

B. Montgomery Pettitt, Ph.D., is the Robert A. Welch Distinguished Chair in Chemistry and Professor in the Departments of Pharmacology and Toxicology and of Biochemistry and Molecular Biology at the University of Texas Medical Branch. He also directs the Sealy Center for Structural Biology and Molecular Biophysics, a research center serving the greater Houston-Galveston area with facilities for structural biology (x-ray, NMR and cryoEM) and scientific computing for use in the areas of simulation and modeling. His research focuses on understanding molecular recognition and folding of biopolymers in solution. His theoretical research interests have led to the development of novel methods for calculating the behavior of biopolymers in solution and near surfaces. He earned his B.S. and Ph.D. from the University of Houston, was a postdoctoral fellow at the University of Texas at Austin, and was an NIH Fellow at Harvard University.

Scott A. Showalter, Ph.D., is an Assistant Professor in the Department of Chemistry at the Pennsylvania State University. Dr. Showalter’s research aims to understand structure-function relationships in biomolecular systems that display extensive conformational dynamics. His group has developed solution NMR spectroscopy methods based on direct carbon detection that enable high resolution structural and dynamic studies of intrinsically disordered proteins and the conformational changes they undergo in folding-upon-binding reaction mechanisms. Combining

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