期刊
CHEMPHYSCHEM
卷 19, 期 19, 页码 2507-2511出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cphc.201800504
关键词
molecular dynamics; intrinsically disordered protein; alpha-synuclein; protein models; structural dynamics
资金
- DFG [DFG-EXC 171, CNMPB A1]
In the absence of a stable fold, transient secondary structure kinetics define the native state of the prototypical and pharmacologically relevant intrinsically disordered protein (IDP) alpha-Synuclein (aS). Here, we investigate kinetics preventing ordering and possibly pathogenic beta-sheet aggregation. Interestingly, transient beta-sheets form frequently at sub s time scales precisely at the positions observed in aS amyloid fibrils. The formation kinetics competes with rapid secondary structure dissociation rates, thus explaining the low secondary structure content. The fast secondary structure dissociation times are very similar to the dynamics of tertiary structure rearrangements. These findings suggest that the fast dissociation kinetics slows down conformational selection processes for aS aggregation, which may be a general mechanism controlling the aggregation kinetics of IDPs.
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