抗冻蛋白
防冻剂
笼状水合物
冰晶
化学
结晶学
蛋白质折叠
蛋白质吸附
吸附
生物化学
水合物
有机化学
物理
光学
作者
Tianjun Sun,Feng-Hsu Lin,Robert L. Campbell,John S. Allingham,Peter L. Davies
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2014-02-14
卷期号:343 (6172): 795-798
被引量:155
标识
DOI:10.1126/science.1247407
摘要
When polypeptide chains fold into a protein, hydrophobic groups are compacted in the center with exclusion of water. We report the crystal structure of an alanine-rich antifreeze protein that retains ~400 waters in its core. The putative ice-binding residues of this dimeric, four-helix bundle protein point inwards and coordinate the interior waters into two intersecting polypentagonal networks. The bundle makes minimal protein contacts between helices, but is stabilized by anchoring to the semi-clathrate water monolayers through backbone carbonyl groups in the protein interior. The ordered waters extend outwards to the protein surface and likely are involved in ice binding. This protein fold supports both the anchored-clathrate water mechanism of antifreeze protein adsorption to ice and the water-expulsion mechanism of protein folding.
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