This paper reviews the molecular theory of hydrophobic effects relevant to
biomolecular structure and assembly in aqueous solution. Recent progress has
resulted in simple, validated molecular statistical thermodynamic theories and
clarification of confusing theories of decades ago. Current work is resolving
effects of wider variations of thermodynamic state, e.g. pressure denaturation
of soluble proteins, and more exotic questions such as effects of surface
chemistry in treating stability of macromolecular structures in aqueous
solutionComment: submitted to Ann. Rev. Phys. Chem., 31 pages, 245 references, 2
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