2005 journal article

Hairpin folding dynamics: The cold-denatured state is predisposed for rapid refolding

BIOCHEMISTRY, 44(30), 10406–10415.

By: R. Dyer n, S. Maness n, S. Franzen n, R. Fesinmeyer n, K. Olsen n & N. Andersen n

MeSH headings : Circular Dichroism; Cold Temperature; Hot Temperature; Humans; Hydrogen Bonding; Kinetics; Magnetic Resonance Spectroscopy; Models, Chemical; Peptides / chemistry; Propanols / chemistry; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Spectroscopy, Fourier Transform Infrared; Thermodynamics
TL;DR: The acceleration of the folding rate of MrH3a in 8% HFIP is interpreted as a direct consequence of the collapsed conformations of the cold-denatured state, and there may be some reduction of the loop search cost when starting from theCold denaturation state, since this state may have some of the stabilizing cross-strand interactions already formed. (via Semantic Scholar)
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