THE HYDROPHOBIC-STAPLE MOTIF AND A ROLE FOR LOOP-RESIDUES IN ALPHA-HELIX STABILITY AND PROTEIN-FOLDING
THE HYDROPHOBIC-STAPLE MOTIF AND A ROLE FOR LOOP-RESIDUES IN ALPHA-HELIX STABILITY AND PROTEIN-FOLDING
复制标题
DOI：
10.1038/nsb0595-380
复制
发表时间：
1995-05-01
期刊：
影响因子：
--
通讯作者：
SERRANO, L
中科院分区：
文献类型：
--
作者：
MUNOZ, V;BLANCO, FJ;SERRANO, L
在α-螺旋的氨基末端描述了一个重复的局部结构基序，其由位于N-帽之前的残基与螺旋内的残基之间的特异性疏水相互作用（i，i+5相互作用）组成。设计的肽的NMR和CD分析证明其在水溶液中的存在，其对α-螺旋稳定性的贡献以及其在限定α-螺旋N末端限制中的作用。将该肽的N-末端结构与具有相同指纹序列的蛋白质的N-末端结构进行比较，发现它们具有惊人的相似性。由该基序引起的多肽链方向的改变表明，位于二级结构元件之间的多肽片段中的残基在蛋白质折叠中起重要作用。
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.