Hydrophobic hydration, hydrophobic forces and protein folding

Philippa M. Wiggins

Physica A: Statistical Mechanics and its Applications, 1997, vol. 238, issue 1, 113-128

Abstract: There is no general agreement about the molecular mechanism of hydrophobic hydration. The preferred models all consider only the state of single water molecules immediately adjacent to the hydrophobic solute to which they cannot hydrogen bond. Because, fortuitously, all experiments, until recently, have been done at room temperature, the large decrease in entropy accompanying hydrophobic hydration has been taken to mean that the phenomenon is “entropy driven” when common sense says that the effect of losing a whole hydrogen bond is a large increase in enthalpy. At higher temperatures, enthalpy does become positive, further confusing interpretation.

Keywords: Hydrophobic; Water; Protein folding; Lipid bilayers; Low-density water (search for similar items in EconPapers)
Date: 1997
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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:238:y:1997:i:1:p:113-128

DOI: 10.1016/S0378-4371(96)00431-1

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