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College Park, Maryland      June 6 - 10 , 2004

WP21: Protein Solvent Coupling in Native and Glass Environments

J. E. Curtis, D. A. Neumann (NIST Center for Neutron Research), D. J. Tobias (Chemistry Department, University of California, Irvine 92697)

Recent experimental and computational studies have conclusively shown that water is essential in the activation of dynamical motions required for biologically relevant protein function. We have found that the microscopic origins of this affect in native environments are directly related to the temperature dependence of the diffusion of water from the protein surface. We are extending our studies of protein dynamics through the use of molecular dynamics simulations of the protein RNase A in both native and non-native glassy environments. We have found that binary glass mixtures can reduce protein dynamics at high temperature. Detailed analysis of the microscopic origins of this effect will be presented.

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