Antifreeze proteins: an unusual receptor-ligand interaction

被引：307

作者：

Jia, ZC ^{[1
]}

Davies, PL ^{[1
]}

机构：

[1] Queens Univ, Dept Biochem, Kingston, ON K7L 3N6, Canada

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2002年 / 27卷 / 02期

基金：

加拿大健康研究院;

关键词：

D O I：

10.1016/S0968-0004(01)02028-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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).

引用

页码：101 / 106

页数：6

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