Please use this identifier to cite or link to this item:
Scopus Web of Science® Altmetric
Type: Journal article
Title: Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding
Author: Huang, D.M.
Chandler, D.
Citation: Proceedings of the National Academy of Sciences of USA, 2000; 97(15):8324-8327
Publisher: National Academy of Sciences
Issue Date: 2000
ISSN: 0027-8424
Statement of
David M. Huang and David Chandler
Abstract: The Lum–Chandler–Weeks theory of hydrophobicity [Lum, K., Chandler, D. & Weeks, J. D. (1999) J. Phys. Chem. 103, 4570–4577] is applied to treat the temperature dependence of hydrophobic solvation in water. The application illustrates how the temperature dependence for hydrophobic surfaces extending less than 1 nm differs significantly from that for surfaces extending more than 1 nm. The latter is the result of water depletion, a collective effect, that appears at length scales of 1 nm and larger. Because of the contrasting behaviors at small and large length scales, hydrophobicity by itself can explain the variable behavior of entropies of protein folding.
Keywords: Solutions
Energy Transfer
Protein Folding
Rights: Copyright © The National Academy of Sciences
DOI: 10.1073/pnas.120176397
Appears in Collections:Aurora harvest 7
Chemistry and Physics publications

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.