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• W2058333742 startingPage "646" @default.
• W2058333742 abstract "A recent study of experimental results for flavodoxin-like folds suggests that proteins from this family may exhibit a similar, signature pattern of folding intermediates. We study the folding landscapes of three proteins from the flavodoxin family (CheY, apoflavodoxin, and cutinase) using a simple nucleation and growth model that accurately describes both experimental and simulation results for the transition state structure, and the structure of on-pathway and misfolded intermediates for CheY. Although the landscape features of these proteins agree in basic ways with the results of the study, the simulations exhibit a range of folding behaviours consistent with two alternate folding routes corresponding to nucleation and growth from either side of the central beta-strand." @default.
• W2058333742 created "2016-06-24" @default.
• W2058333742 creator A5039591575 @default.
• W2058333742 creator A5045320008 @default.
• W2058333742 date "2006-05-01" @default.
• W2058333742 modified "2023-10-14" @default.
• W2058333742 title "Alternate Pathways for Folding in the Flavodoxin Fold Family Revealed by a Nucleation-growth Model" @default.
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• W2058333742 doi "https://doi.org/10.1016/j.jmb.2006.02.026" @default.
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