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• W2071494327 abstract "Abstract Elucidating the mechanism for the fast folding of proteins is a challenging task. In our earlier work, we introduced the concept of “long‐range order” and related it successfully to protein folding rates. In this article, we propose a new hypothesis for the folding of two‐state all‐β proteins. The mechanism is based on the formation of a hydrophobic core, propagation of β‐strands, and the establishment of hydrogen bonds. Our hypothesis has been strengthened by the observation of a folding nucleus in β‐strands and the hydrogen‐bonding network between residues in β‐strands. Our insights on protein folding show an excellent agreement with experimental observations." @default.
• W2071494327 created "2016-06-24" @default.
• W2071494327 creator A5046879365 @default.
• W2071494327 creator A5071391614 @default.
• W2071494327 date "2004-12-31" @default.
• W2071494327 modified "2023-09-27" @default.
• W2071494327 title "Folding Mechanism of All‐β Globular Proteins" @default.
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• W2071494327 doi "https://doi.org/10.1081/pb-120027110" @default.
• W2071494327 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15046294" @default.
• W2071494327 hasPublicationYear "2004" @default.
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