THE HYDROPHOBIC-STAPLE MOTIF AND A ROLE FOR LOOP-RESIDUES IN ALPHA-HELIX STABILITY AND PROTEIN-FOLDING

被引：122

作者：

MUNOZ, V ^{[1
]}

BLANCO, FJ ^{[1
]}

SERRANO, L ^{[1
]}

机构：

[1] EUROPEAN MOLEC BIOL LAB, D-69012 HEIDELBERG, GERMANY

来源：

NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 05期

关键词：

D O I：

10.1038/nsb0595-380

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：

A recurrent local structural motif is described at the amino terminus of alpha-helices, that consists of a specific hydrophobic interaction between a residue located before the N-cap, with a residue within the helix (i,i+5 interaction). NMR and CD analysis of designed peptides demonstrate its presence in aqueous solution, its contribution to alpha-helix stability and its role in defining the alpha-helix N terminus limit. Comparison between the N-terminal structures of the peptide and those in proteins with the same fingerprint sequence, shows striking similarities, The change in the polypeptide chain direction produced by the motif suggests an important role in protein folding for residues located in polypeptide segments between secondary structure elements.

引用

页码：380 / 385

页数：6

共 30 条

[1] PRINCIPLES THAT GOVERN FOLDING OF PROTEIN CHAINS [J].