Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding

Journal Article · Sat Apr 01 04:00:00 EST 2000 · Proceedings of the National Academy of Sciences

DOI:https://doi.org/10.1073/pnas.120176397· OSTI ID:843045

Huang, David M ^[1]; Chandler, David

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1. LBNL Library

The Lum-Chandler-Weeks theory of hydrophobicity [J. Phys. Chem. 103, 4570 (1999)] 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 1nm differs significantly from that for surfaces extending more than 1nm. The latter is the result of water depletion, a collective effect, that appears at length scales of 1nm and larger. Due to the contrasting behaviors at small and large length scales, hydrophobicity by itself can explain the variable behavior of protein folding.

• Research Organization: Ernest Orlando Lawrence Berkeley National Laboratory, Berkeley, CA (US)
• Sponsoring Organization: USDOE Director, Office of Science. Office of Basic Energy Sciences
• DOE Contract Number: AC03-76SF00098
• OSTI ID: 843045
• Report Number(s): LBNL--45485
• Journal Information: Proceedings of the National Academy of Sciences, Journal Name: Proceedings of the National Academy of Sciences Journal Issue: 15 Vol. 97
• Country of Publication: United States
• Language: English

Related Subjects

37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY
59 BASIC BIOLOGICAL SCIENCES
PROTEINS
SOLVATION
TEMPERATURE DEPENDENCE
WATER
solvation hydrophobic effect temperature length scale dependence protein folding