期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 27, 期 2, 页码 101-106出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/S0968-0004(01)02028-X
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Antifreeze proteins (AFPs) help organisms to survive below 0degreesC by inhibiting ice growth. Although AFPs are structurally diverse, they typically present a large proportion of their surface area for binding to ice. Whereas earlier proposed binding mechanisms relied almost entirely on a hydrogen bond match between the AFP and ice, it now seems probable that van der Waals and hydrophobic interactions make a significant contribution to the enthalpy of adsorption. These interactions require intimate surface-surface complementarity between the receptor (AFP) and its ligand (ice).
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