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Talk, Christopher Paeslack

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  • cmb seminar
When May 08, 2017
from 11:00 AM to 12:30 PM
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Characterization of collective protein-water-membrane dynamics

Water is ubiquitous in all living organisms and an essential component in cellular environments1.     It is the natural solvent in manifold biological processes and contributes to the  stabilization of native protein structures and protein dynamics2. Therefore, a detailed description of solute-solvent interactions is necessary not only to understand static and thermodynamic properties of biomolecules, but also their dynamics. Studying the dynamical perturbation of protein hydration water is a direct probe for collective protein-water dynamics under native conditions. In this work, we investigate correlations of vibrational motion on the surface of proteins and lipid bilayers with their hydration shells. To this end, we analyze the distribution of correlated longitudinal motions in the three-dimensional environment of the solute as a function of frequency.  We obtain longitudinal velocity current spectra that were previously found to show dispersive behavior when visualized in k-space (k = 2๐œ‹/r), i.e. there is a spatial dependence of correlated protein-water collective hydrogen-bond dynamics3. Such longitudinal current spectra describe spatially correlated density ๏ฌ‚uctuations and can be linked to the experimentally accessible dynamic structure factor S(k,๐œ”) via IJ(๐œ”,k) = (๐œ”2/k2) S(k,๐œ”). We seek to understand (1) which role such collective vibrational motion splay in biomolecular binding, and (2) how our results can be linked to observables assessed by coherent neutron scattering.
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