CONFORMATIONAL-ANALYSIS OF THE BACKBONE-DEPENDENT ROTAMER PREFERENCES OF PROTEIN SIDE-CHAINS

被引：275

作者：

DUNBRACK, RL ^{[1
]}

KARPLUS, M ^{[1
]}

机构：

[1] HARVARD UNIV,DEPT CHEM,CAMBRIDGE,MA 02138

来源：

NATURE STRUCTURAL BIOLOGY | 1994年 / 1卷 / 05期

关键词：

D O I：

10.1038/nsb0594-334

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：

Amino acids have sidechain rotamer preferences dependent on the backbone dihedral angles phi and psi. These preferences provide a method for rapid structure prediction which is a significant improvement over backbone-independent rotamer libraries. We demonstrate here that simple arguments based on conformational analysis can account for many of the features of the observed backbone dependence of the sidechain rotamers. Steric repulsions corresponding to the 'butane' and 'syn-pentane' effects make certain conformers rare, as has been observed experimentally.

引用

页码：334 / 340

页数：7

共 32 条

[1] CONFORMATIONAL ENERGIES OF N-ALKANES AND RANDOM CONFIGURATION OF HIGHER HOMOLOGS INCLUDING POLYMETHYLENE [J].