...
  • 主题
高级搜索  >
历史搜索 清空历史
首页> 外文期刊>Biochemistry >Structure and dynamics of beta-helical antifreeze protein
【24h】

Structure and dynamics of beta-helical antifreeze protein

机译：β-螺旋抗冻蛋白的结构和动力学

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

Antifreeze proteins (AFPs) protect many types of organisms from damage caused by freezing. They do this by binding to the ice surface, which causes inhibition of ice crystal growth. However, the molecular mechanism of ice binding leading to growth inhibition is not well understood. In this paper, we present the solution structure and backbone NMR relaxation data of the antifreeze protein from the yellow mealworm beetle Tenebrio molitor (TmAFP) to study the dynamics in the context of structure. The full N-15 relaxation analysis was completed at two magnetic field strengths, 500 and 600 MHz, as well as at two temperatures, 30 and 5 degreesC, to measure the dynamic changes that occur in the protein backbone at different temperatures. TmAFP is a small, highly disulfide-bonded, right-handed parallel beta-helix consisting of seven tandemly repeated 12-amino acid loops. The backbone relaxation data displays a periodic pattern, which reflects both the 12-amino acid structural repeat and the highly anisotropic nature of the protein. Analysis of the N-15 relaxation parameters shows that TmAFP is a well-defined, rigid structure, and the extracted parameters show that there is similar restricted internal mobility throughout the protein backbone at both temperatures studied. We conclude that the hydrophobic, rigid binding site may reduce the entropic penalty for the binding of the protein to ice. The beta-helical fold of the protein provides this rigidity, as it does not appear to be a consequence of cooling toward a physiologically relevant temperature. [References: 62]
机译：抗冻蛋白（AFP）保护许多类型的生物免受冻结造成的损害。它们通过与冰表面结合来实现此目的，从而导致冰晶生长受到抑制。但是，关于冰结合导致生长抑制的分子机理尚不清楚。在本文中，我们提供了来自黄粉虫甲虫黄粉虫（TmAFP）的抗冻蛋白的溶液结构和骨架NMR弛豫数据，以研究结构中的动力学。完整的N-15弛豫分析在500和600 MHz的两个磁场强度以及30和5摄氏度的两个温度下完成，以测量在不同温度下蛋白质骨架中发生的动态变化。 TmAFP是一个小的，高度二硫键的右旋平行β螺旋，由七个串联重复的12个氨基酸环组成。主链弛豫数据显示出周期性模式，该模式既反映了12个氨基酸的结构重复，又反映了蛋白质的高度各向异性。对N-15弛豫参数的分析表明，TMAFP是一个定义明确的刚性结构，而提取的参数表明，在所研究的两个温度下，整个蛋白质主链都有相似的受限内部迁移率。我们得出的结论是，疏水性，刚性结合位点可以减少蛋白质与冰结合的熵损失。蛋白质的β螺旋折叠提供了这种刚性，因为它似乎不是冷却至生理相关温度的结果。 [参考：62]

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