Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding.
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.
Huang
D M
DM
Department of Chemistry, University of California, Berkeley, CA 94720, USA.
Chandler
D
D
D004735:Energy Transfer; D017510:Protein Folding; D012996:Solutions; D013696:Temperature
D012996:Solutions