Complementary packing of α-helices in proteins

被引：31
作者：
Efimov, AV [1 ]
机构：
[1] Russian Acad Sci, Inst Prot Res, Pushchino 142292, Moscow Region, Russia
来源：
FEBS LETTERS | 1999年 / 463卷 / 1-2期
关键词：
complementarity; helix packing; hydrophobic stripe; packing angle; protein structure;
D O I：
10.1016/S0014-5793(99)01507-0
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：
The packing of alpha-helices in proteins is restricted by both the principle of close packing and the chemical nature of side chains. As a result, (1) a-helical surfaces forming the interface should be complementary to each other, (2) hydrophobic stripes of the alpha-helices should fit together like pieces of a jigsaw puzzle, and (3) buried polar side chains (if there are any) should be arranged in a complementary fashion, (C) 1999 Federation of European Biochemical Societies.
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页码：3 / 6
页数：4
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