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.

引用

页码：3 / 6

页数：4

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