Hairpin Folding Dynamics: The Cold-Denatured State Is Predisposed for Rapid Refolding
Dyer, R. B., Maness, S. J., Franzen, S., Fesinmeyer, R. M., Olsen, K. A., & Andersen, N. H. (2005, July 6). Biochemistry, Vol. 44, pp. 10406–10415.
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
topics (OpenAlex): Protein Structure and Dynamics; Enzyme Structure and Function; Mass Spectrometry Techniques and Applications
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.
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