Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/87359
Citations | ||
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. Chandler, D. |
Citation: | Proceedings of the National Academy of Sciences of the United States Of America, 2000; 97(15):8324-8327 |
Publisher: | National Academy of Sciences |
Issue Date: | 2000 |
ISSN: | 0027-8424 1091-6490 |
Statement of Responsibility: | 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; Temperature; Energy Transfer; Protein Folding |
Rights: | Copyright © The National Academy of Sciences |
DOI: | 10.1073/pnas.120176397 |
Appears in Collections: | 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.