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- W2111852022 endingPage "1746" @default.
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- W2111852022 abstract "Abstract Isolated β‐hairpins in water have a temperature dependence of their conformational stability qualitatively resembling that of globular proteins, showing both cold and hot unfolding transitions. It is shown that a molecular‐level rationalization of this cold unfolding can be provided extending the approach devised for globular proteins (Graziano G. Phys Chem Chem Phys 2010; 12:14245‐14252). The decrease in the solvent‐excluded volume upon folding, measured by the decrease in the solvent accessible surface area, produces a gain in configurational/translational entropy of water molecules that is the main stabilizing contribution of the folded conformation. This always stabilizing Gibbs energy contribution has a parabolic‐like temperature dependence in water and is exactly counterbalanced at two temperatures (i.e., the cold and hot unfolding temperatures) by the always destabilizing Gibbs energy contribution due to the loss in conformational degrees of freedom of the peptide chain. Proteins 2011; © 2011 Wiley‐Liss, Inc." @default.
- W2111852022 created "2016-06-24" @default.
- W2111852022 creator A5056333763 @default.
- W2111852022 creator A5072720343 @default.
- W2111852022 date "2011-04-04" @default.
- W2111852022 modified "2023-10-17" @default.
- W2111852022 title "Cold unfolding of β-hairpins: A molecular-level rationalization" @default.
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- W2111852022 doi "https://doi.org/10.1002/prot.22997" @default.
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