Stabilization of the N-terminal beta-hairpin of ubiquitin by a terminal hydrophobic cluster.
Stabilization of the N-terminal beta-hairpin of ubiquitin by a terminal hydrophobic cluster.
复制标题
通过末端疏水簇稳定泛素的 N 末端 β-发夹。
DOI：
10.1002/bip.20840
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发表时间：
2008
期刊：
影响因子：
2.9
通讯作者：
Waters,MarceyL
中科院分区：
文献类型：
--
作者：
Riemen,AlexJ;Waters,MarceyL
对模型 β-发夹肽的研究可以更好地了解参与蛋白质 β-折叠二级结构形成的因素。众所周知，转角序列、侧链-侧链相互作用、链间氢键和残基的β-折叠倾向对于水溶液中的β-发夹稳定性都很重要。然而，发夹末端残基侧链的相互作用被认为对整体发夹稳定性贡献甚微，因为这些残基通常会磨损。在这里，作者报告了在天然存在的切除的泛素 N 末端 β 发夹的末端有一个稳定的疏水性残基簇，该残基在水溶液中自主折叠。我们的数据表明，从该发夹中删除 Met1 和 Val17 会破坏水溶液和甲醇水溶液中折叠状态的稳定性。这些结果表明，通常磨损的末端残基的相互作用仍然可以显着促进 β-发夹的整体稳定性。 © 2007 Wiley periodicals, Inc. Biopolymers (Pept Sci) 90: 394–398, 2008。本文最初作为已接受的预印本在线发表。 “在线发布”日期对应于预印本版本。您可以通过发送电子邮件至 Biopolymers 编辑部索取预印本副本：biopolymers@wiley.com
Study of model β‐hairpin peptides allows for better understanding of the factors involved in the formation of β‐sheet secondary structure in proteins. It is known that turn sequence, sidechain–sidechain interactions, interstrand hydrogen bonding, and β‐sheet propensity of residues are all important for β‐hairpin stability in aqueous solution. However, interactions of the sidechains of the terminal residues of hairpins are thought to contribute little to overall hairpin stability since these residues are typically frayed. Here, the authors report a stabilizing hydrophobic cluster of residues at the termini of the naturally occurring excised N‐terminal β‐hairpin of Ubiquitin that folds autonomously in aqueous solution. Our data show that deletion of Met1 and Val17 from this hairpin destabilized the folded state in both aqueous solution and in aqueous‐methanol solutions. These results suggest that interactions of terminal residues which are usually frayed can nonetheless contribute significantly to overall stability of β‐hairpin. © 2007 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 90: 394–398, 2008.This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com