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Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding
Author(s) -
David M. Huang,
David Chandler
Publication year - 2000
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.120176397
Subject(s) - solvation , folding (dsp implementation) , chemical physics , hydrophobic effect , length scale , chemistry , protein folding , entropic force , scale (ratio) , crystallography , thermodynamics , physics , molecule , organic chemistry , mechanics , biochemistry , quantum mechanics , electrical engineering , engineering
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.

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