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• W2113991454 abstract "Molecular dynamics simulations of protein folding can provide very high-resolution data on the folding process; however, due to computational challenges most studies of protein folding have been limited to small peptides, or made use of approximations such as Gō potentials or implicit solvent models. We have performed a set of molecular dynamics simulations totaling >50 μs on the villin headpiece subdomain, one of the most stable and fastest-folding naturally occurring proteins, in explicit solvent. We find that the wild-type villin headpiece reliably folds to a native conformation on timescales similar to experimentally observed folding, but that a fast folding double-norleucine mutant shows significantly more heterogeneous behavior. Along with other recent simulation studies, we note the occurrence of nonnative structures intermediates, which may yield a nativelike signal in the fluorescence measurements typically used to study villin folding. Based on the wild-type simulations, we propose alternative approaches to measure the formation of the native state." @default.
• W2113991454 created "2016-06-24" @default.
• W2113991454 creator A5029996336 @default.
• W2113991454 creator A5031996829 @default.
• W2113991454 date "2009-10-01" @default.
• W2113991454 modified "2023-10-17" @default.
• W2113991454 title "Common Structural Transitions in Explicit-Solvent Simulations of Villin Headpiece Folding" @default.
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• W2113991454 doi "https://doi.org/10.1016/j.bpj.2009.08.012" @default.
• W2113991454 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2764099" @default.
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• W2113991454 hasPublicationYear "2009" @default.
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