• 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Journal of Molecular Biology >The molecular basis for the inverse temperature transition of elastin
【24h】

The molecular basis for the inverse temperature transition of elastin

机译：弹性蛋白逆温度转变的分子基础

获取原文
获取原文并翻译 | 示例
           
页面导航
  • 摘要
  • 著录项
  • 相似文献
  • 相关主题

摘要

Elastin undergoes an "inverse temperature transition" such that it becomes more ordered as the temperature increases. To investigate the molecular basis for this behavior, molecular dynamics simulations were conducted above and below the transition temperature. Simulations of a 90-residue elastin peptide, (VPGVG)(18), with explicit water molecules were performed at seven different temperatures between 7 and 42 degreesC, for a total of 80 ns. Beginning from an idealized P-spiral structure, hydrophobic collapse was observed over a narrow temperature range in the simulations. Moreover, simulations above and below elastin's transition temperature indicate that elastin has more turns and distorted beta -structure at higher temperatures. Water was critical to the inverse temperature transition and elastin-associated water molecules can be divided into three categories: those closely associated with beta II turns; those that form hydrogen bonds with the main-chain groups; and those hydrating the hydrophobic side-chains. Water-swollen, monomeric elastin above the transition temperature is best described as a compact amorphous structure with distorted beta -strands, fluctuating turns, buried hydrophobic residues, and main-chain polar atoms that participate in hydrogen bonds with water. Below the transition temperature, elastin is expanded with similar to 40% local beta -spiral structure. Overall the simulations are in agreement with experiment and therefore appear to provide an atomic-level description of the conformational properties of elastin monomers and the basis for their elastomeric properties.
机译：弹性蛋白经历“逆温度转变”，使得其随着温度升高变得更有序。为了研究这种行为的分子基础，在转变温度之上和之下进行了分子动力学模拟。在7至42摄氏度之间的七个不同温度下，对具有90个残基的弹性蛋白肽（VPGVG）（18）进行了模拟，总计80 ns。从理想的P螺旋结构开始，在狭窄的温度范围内观察到疏水塌陷。此外，在弹性蛋白的转变温度之上和之下的模拟表明，弹性蛋白在更高的温度下具有更多的匝数和扭曲的β结构。水是逆温度转变的关键，而与弹性蛋白相关的水分子可分为三类：与βII转角密切相关的分子;与主链基团形成氢键的那些;和那些能使疏水性侧链水合的物质。过渡温度以上的水溶胀的单体弹性蛋白最好描述为一种紧凑的无定形结构，具有扭曲的β链，起伏波动，掩埋的疏水残基和参与与水形成氢键的主链极性原子。在转变温度以下，弹性蛋白膨胀，具有类似于40％的局部β螺旋结构。总体而言，模拟与实验一致，因此似乎提供了弹性蛋白单体构象性质的原子级描述及其弹性体性质的基础。

著录项

相似文献

  • 外文文献
  • 中文文献
  • 专利
获取原文

客服邮箱：kefu@zhangqiaokeyan.com

京公网安备：11010802029741号 ICP备案号：京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有

  • 客服微信

  • 服务号