Folding minimal sequences: the lower bound for sequence complexity of globular proteins

被引：60

作者：

Romero, P

Obradovic, Z

Dunker, AK ^{[1
]}

机构：

[1] Washington State Univ, Sch Mol Biosci, Pullman, WA 99164 USA

[2] Washington State Univ, Sch Elect Engn & Comp Sci, Pullman, WA 99164 USA

来源：

FEBS LETTERS | 1999年 / 462卷 / 03期

基金：

美国国家科学基金会;

关键词：

protein folding; minimal sequence; complexity; alphabet size; entropy;

D O I：

10.1016/S0014-5793(99)01557-4

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：

Alphabet size and informational entropy, two formal measures of sequence complexity, are herein applied to two prior studies on the folding of minimal proteins. These measures show a designed four-helix bundle to be unlike its natural counterparts but rather more like a coiled-coil dimer, Segments from a simplified sarc homology 3 domain and more than 2000000 segments from globular proteins both have lower bounds for alphabet size of 10 and for entropy near 2.9, These values are therefore suggested to be necessary and sufficient for folding into globular proteins having both rigid side chain packing and biological function. (C) 1999 Federation of European Biochemical Societies.

引用

页码：363 / 367

页数：5

共 23 条

[1]

ABOLA EE, 1987, CRYSTALLOGRAPHIC DAT, P107

[2] The SWISS-PROT protein sequence data bank and its supplement TrEMBL in 1999 [J].