| Literature DB >> 11972014 |
Abstract
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 solution.Year: 2002 PMID: 11972014 DOI: 10.1146/annurev.physchem.53.090401.093500
Source DB: PubMed Journal: Annu Rev Phys Chem ISSN: 0066-426X Impact factor: 12.703