Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding
Date
2000
Authors
Huang, D.
Chandler, D.
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Journal article
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Proceedings of the National Academy of Sciences of the United States Of America, 2000; 97(15):8324-8327
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David M. Huang and David Chandler
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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.
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Copyright © The National Academy of Sciences