期刊
PHYSICAL REVIEW LETTERS
卷 110, 期 16, 页码 -出版社
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.110.168103
关键词
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资金
- CINECA award under the ISCRA initiative
- FIRB-Futuro in Ricerca, Progetto [RBAP11ETKA_004]
By extended atomistic simulations in explicit solvent and bias-exchange metadynamics, we study the aggregation process of 18 chains of the C-terminal segment of amyloid-beta, an intrinsically disordered protein involved in Alzheimer's disease and prone to form fibrils. Starting from a disordered aggregate, we are able to observe the formation of an ordered nucleus rich in beta sheets. The rate limiting step in the nucleation pathway involves crossing a barrier of approximately 40 kcal/mol and is associated with the formation of a very specific interdigitation of the side chains belonging to different sheets. This structural pattern is different from the one observed experimentally in a microcrystal of the same system, indicating that the structure of a nascent'' fibril may differ from the one of an extended'' fibril. DOI: 10.1103/PhysRevLett.110.168103
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