A MODEL FOR BINDING OF AN ANTIFREEZE POLYPEPTIDE TO ICE

被引：140
|
作者：
WEN, DY [1 ]
LAURSEN, RA [1 ]
机构：
[1] BOSTON UNIV,DEPT CHEM,590 COMMONWEALTH AVE,BOSTON,MA 02215
来源：
BIOPHYSICAL JOURNAL | 1992年 / 63卷 / 06期
关键词：
D O I：
10.1016/S0006-3495(92)81750-2
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
A model is proposed, based on recent peptide analog and ice crystal etching studies, whereby an alanine-rich, alpha-helical antifreeze polypeptide (AFP) from the winter flounder inhibits the growth of ice crystals by hydrogen bonding of Thr, Asn, and Asp side chains in a specific pattern to the {2021BAR} hexagonal bipyramidal planes of ice. It is further suggested that this mode of binding is unidirectional, maximizing opportunities for packing of AFPs, on the ice surface, and that ice crystal growth inhibition occurs by a two-step mechanism involving hydrogen bonding and hydrophobic interpeptide interactions.
引用
收藏
页码：1659 / 1662
页数：4
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