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

@article{Huang2000TemperatureAL,
  title={Temperature and length scale dependence of hydrophobic effects and their possible implications for protein folding.},
  author={Danrun Huang and David Chandler},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 15},
  pages={8324-7}
}
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… CONTINUE READING

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Schematic of protein-folding equilibrium. The black and white circles represent hydrophobic and hydrophilic residues, respectively. The shaded region depicts aqueous solution

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