Triplet–triplet energy transfer studies on conformational dynamics in peptides and a protein-猫眼课题宝

肽和蛋白质构象动力学的三重态-三重态能量转移研究

DOI：

发表时间：

2011

期刊：

Journal of Peptide Science

影响因子：

2.1

通讯作者：

中科院分区：

生物学4区

文献类型：

作者：

Andreas Reiner

肽和蛋白质是高度动态的系统，其可以采用或多或少稳定的构象。这些分子的动力学，特别是那些在纳秒到几十微秒的时间尺度上的分子，很难用常规技术进行评估。本文综述了使用TTET的实验，该技术报告了三重态供体和受体基团之间的货车范德华接触形成，并且在此时间范围内是敏感的。TTET允许直接测量非结构化模型肽的链动力学，即纳秒时间尺度上的大幅波动。此外，接触形成可以作为不可逆的探测反应来研究构象平衡的动力学。这种方法使我们能够测量螺旋肽中的局部α-螺旋折叠和解折叠，这为这一基本二级结构元件的平衡动力学提供了新的见解。TTET也被应用于研究蛋白质的天然和未折叠状态的动力学，绒毛膜头片段亚结构域。不同位置之间的接触形成动力学揭示了解锁和本地解折叠反应在本模型蛋白质的天然状态，并给出了信息的链动力学在未折叠状态合奏。版权所有© 2011欧洲肽协会和约翰威利父子有限公司。

Peptides and proteins are highly dynamic systems, which can adopt more or less stable conformations. The dynamics of these molecules, particularly those on the nanosecond to tens of microsecond time scale, are difficult to assess with conventional techniques. This review summarizes experiments using TTET, a technique that reports on van der Waals contact formation between a triplet donor and acceptor group, and which is sensitive in this time range. TTET allows to directly measure the chain dynamics of unstructured model peptides, i.e. large‐amplitude fluctuations on the nanosecond time scale. Furthermore, contact formation can be used as irreversible probing reaction to study the kinetics of conformational equilibria. This approach enabled us to measure local α‐helix folding and unfolding in helical peptides, which gave new insight into the equilibrium dynamics of this fundamental secondary structure element. TTET has also been applied to study the dynamics both in the native and unfolded state of a protein, the villin headpiece subdomain. The contact formation kinetics between different positions revealed an unlocking and local unfolding reaction in the native state of this model protein, and gave information about the chain dynamics in the unfolded state ensemble. Copyright © 2011 European Peptide Society and John Wiley & Sons, Ltd.