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BP: Fachverband Biologische Physik

BP 24: Posters - Protein Structure and Dynamics

BP 24.9: Poster

Dienstag, 21. März 2017, 14:00–16:00, P1A

MD Simulation Studies of Protein Dynamics in Neutral Confinement — •Timothy Wohlfromm, Matthias Bartelmeß, Tatjana Thiel, and Michael Vogel — Institut für Festkörperphysik, TU Darmstadt, Hochschulstraße 6, 64289 Darmstadt, Germany

We report on recent findings regarding dynamics of the elastin like protein model (VPGVG)₅₀ and its surrounding hydration shell in a neutral pore. Despite recent progress we lack understanding of dynamics of complex systems, such as proteins, specifically when studied in confinement. To isolate direct effects of confining geometries on protein dynamics the pore consists of the same atom type as the solvent, in most cases water, restrained in position by harmonic potentials of varying restoring forces to simulate confining surfaces with differing rigidity. Varying the hydration level of the confined protein we find that the minimal degree of hydration as ratio of water mass to protein mass for the protein to show bulk behaviour is 1 g/g. Moreover, we observe in spatially resolved analyses that with decreasing distance to the pore wall the correlation times of water increase by more than one order of magnitude. This effect is drastically reduced with reduced rigidity of the pore wall. In addition the protein acts as a soft confinement to water in vicinity to its surface. Finally, we systematically investigate changes in the dynamics of the elastin model when water is replaced by other solvents.