Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i, i + 4.
Helix-stabilizing interaction between tyrosine and leucine or valine when the spacing is i, i + 4.
复制标题
当间距为 i, i 4 时，酪氨酸和亮氨酸或缬氨酸之间的螺旋稳定相互作用。
DOI：
10.1006/jmbi.1994.1545
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发表时间：
1994
影响因子：
5.6
通讯作者：
Baldwin,RL
中科院分区：
文献类型：
--
作者：
Padmanabhan,S;Baldwin,RL
当间距为i，i+4时，已在基于丙氨酸的肽螺旋中发现酪氨酸与亮氨酸或缬氨酸之间的螺旋稳定相互作用。对照肽具有相同的组成，但间隔为i，i，+3。据我们所知，这是第一次报告的螺旋稳定的相互作用之间的两个非极性侧链在一个孤立的螺旋。结果解释了为什么在早期的研究中，亮氨酸被发现具有类似于丙氨酸的螺旋倾向，而后来来自另一个实验室和我们自己的工作表明丙氨酸比亮氨酸在丙氨酸基肽中的螺旋更稳定。在螺旋含量的变化所造成的thei，i，+ 4 Tyr？Leu相互作用与侧链对之间的其他特定相互作用（如离子对或Phe · His+相互作用）的变化相当。
A helix-stabilizing interaction between tyrosine and leucine or valine has been found in alanine-based peptide helices when the spacing is i,i+4. Control peptides have identical compositions but an i,i,+3 spacing. This is, to our knowledge, the first report of a helix-stabilizing interaction between two non-polar side-chains in an isolated helix. The results explain why, in an earlier study, leucine was found to have a helix propensity similar to that of alanine in an alanine-based peptide, whereas later work from another laboratory and our own has shown that alanine is markedly more helix-stabilizing than leucine in alanine-based peptides. The change in helix content resulting from thei,i, + 4 Tyr?Leu interaction is comparable to the changes seen for other specific interactions between pairs of side-chains, such as ion-pair or Phe · His+interactions.