IDENTIFICATION OF PROTEIN FOLDS - MATCHING HYDROPHOBICITY PATTERNS OF SEQUENCE SETS WITH SOLVENT ACCESSIBILITY PATTERNS OF KNOWN STRUCTURES

被引：89

作者：

BOWIE, JU

CLARKE, ND

PABO, CO

SAUER, RT

机构：

[1] MIT,DEPT BIOL,77 MASSACHUSETTS AVE,CAMBRIDGE,MA 02139

[2] JOHNS HOPKINS UNIV,SCH MED,HOWARD HUGHES MED INST,BALTIMORE,MD 21205

[3] JOHNS HOPKINS UNIV,SCH MED,DEPT MOLEC BIOL & GENET,BALTIMORE,MD 21205

来源：

PROTEINS-STRUCTURE FUNCTION AND GENETICS | 1990年 / 7卷 / 03期

关键词：

protein families; structure prediction;

D O I：

10.1002/prot.340070307

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：

Hydrophobic side chains often are buried in the interior of a protein, and evolutionarily related proteins usually maintain the hydrophobic character of buried position. In this paper we shown that a pattern of hydrophobicity values derived from a set of related protein sequences is well correlated with the linear pattern of side‐chain solvent accessibility values, calculated from a known protein structure representative of the sequences. In several cases, information from aligned sequences can be used to select the correct tertiary fold from a large database of protein structures. Copyright © 1990 Wiley‐Liss, Inc.

引用

页码：257 / 264

页数：8

共 29 条

[1] RECOGNITION OF A DNA OPERATOR BY THE REPRESSOR OF PHAGE-434 - A VIEW AT HIGH-RESOLUTION [J].