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AKB: Biologische Physik

AKB 90: Protein Folding and Molecular Dynamics

AKB 90.4: Vortrag

Mittwoch, 9. März 2005, 14:45–15:00, TU H2013

How parallel is protein (un)folding? — •Lothar Reich and Thomas R. Weikl — Max Planck Institute of Colloids and Interfaces, Theory Division, 14424 Potsdam

According to the ‘old view’, proteins fold along well-defined sequential pathways, whereas the ‘new view’ sees protein folding as a highly parallel stochastic process on funnel-shaped energy landscapes. We have analyzed parallel and sequential processes on a large number of Molecular Dynamics unfolding trajectories for the protein CI2 at high temperatures. Using rigorous statistical measures, we find that the degree of sequentiality depends on the structural level under consideration. On a coarse substructural level of whole β-sheets and helices, unfolding is predominantly sequential. In contrast, the unfolding process is more parallel on the level of individual contacts between the residues of the protein chain. On an intermediate structural level, the characteristic parallel and sequential events can be understood from simple loop-closure dependencies between the substructural elements.