TESTS FOR HELIX-STABILIZING INTERACTIONS BETWEEN VARIOUS NONPOLAR SIDE-CHAINS IN ALANINE-BASED PEPTIDES

被引：90

作者：

PADMANABHAN, S ^{[1
]}

BALDWIN, RL ^{[1
]}

机构：

[1] STANFORD UNIV,SCH MED,BECKMAN CTR,DEPT BIOCHEM,STANFORD,CA 94305

来源：

PROTEIN SCIENCE | 1994年 / 3卷 / 11期

关键词：

ALPHA-HELIX STABILITY; NONPOLAR INTERACTIONS; PEPTIDE HELICES; SIDE-CHAIN CONFORMATION; SIDE-CHAIN INTERACTIONS;

D O I：

10.1002/pro.5560031111

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：

Straight-chain, non-natural, nonpolar amino acids norleucine, norvaline, and alpha-amino-n-butyric acid at various spacings do not interact with themselves to stabilize helix formation in alanine-based peptides, but do interact with a Tyr spaced i, i+4 to stabilize alanine helices, similar to the helix-stabilizing i, i+4 Tyr-Leu and Tyr-Val interactions reported earlier (Padmanabhan S, Baldwin RL, 1994, J Mol Biol 241:706-713). Leu spaced i, i+4 from another Leu is measurably helix-stabilizing relative to the corresponding i, i+3 pair, but less so than for i, i+4 Val-Leu, Ile-Leu, or Phe-Leu pairs (relative to the corresponding i, i+3 pairs) when Leu is C-terminal to the other nonpolar amino acid. Our results indicate that limited side-chain flexibility in an alpha-helix strongly favors the interaction between 2 nonpolar residues to stabilize an isolated alpha-helix.

引用

页码：1992 / 1997

页数：6

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