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- W2023696920 endingPage "1701" @default.
- W2023696920 startingPage "1691" @default.
- W2023696920 abstract "The experimentally well-established folding mechanism of the src-SH3 domain, and in particular the ϕ-value analysis of its transition state, represents a sort of testing table for computational investigations of protein folding. Here, parallel molecular dynamics simulations of the src-SH3 domain have been performed starting from denatured conformations. By rescuing and restarting only trajectories approaching the folding transition state, an ensemble of conformations was obtained with a completely structured central β-sheet and a native-like packing of residues Ile-110, Ala-121, and Ile-132. An analysis of the trajectories shows that there are several pathways leading to the formation of the central β-sheet whereas its two hairpins form in a different but consistent way." @default.
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- W2023696920 date "2004-03-01" @default.
- W2023696920 modified "2023-09-28" @default.
- W2023696920 title "Formation of the Folding Nucleus of an SH3 Domain Investigated by Loosely Coupled Molecular Dynamics Simulations" @default.
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- W2023696920 doi "https://doi.org/10.1016/s0006-3495(04)74238-1" @default.
- W2023696920 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1304005" @default.
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