Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.
Infrared and Fluorescence Assessment of Protein Dynamics: From Folding to Function.
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DOI：
10.1021/acs.jpcb.6b03199
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发表时间：
2016-06-16
期刊：
影响因子：
--
通讯作者：
Gai F
中科院分区：
文献类型：
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作者：
Ding B;Hilaire MR;Gai F
当折叠或执行功能时，蛋白质可以采样丰富的构象空间集。然而，实验捕捉所有的重要运动与足够的细节，让他们的动态力学描述是不平凡的，因为这样的构象事件往往发生在很宽的时间和长度尺度。因此，许多方法已被用来评估蛋白质的构象动力学，根据所讨论的构象转变的性质，一些可能比其他更有利。在这里，我们描述了我们最近的努力，也是其他人，在适当的情况下，使用红外和荧光为基础的技术来询问蛋白质折叠和功能动力学。具体来说，我们专注于讨论如何使用外来光谱探针，以提高这些技术的结构分辨率，以及如何利用各种交联策略，以获得动态和机械信息，以前很难达到。
While folding or performing functions, a protein can sample a rich set of conformational space. However, experimentally capturing all of the important motions with sufficient detail to allow a mechanistic description of their dynamics is nontrivial since such conformational events often occur over a wide range of time and length scales. Therefore, many methods have been employed to assess protein conformational dynamics and, depending on the nature of the conformational transition in question, some may be more advantageous than others. Herein, we describe our recent efforts, and also those of others, wherever appropriate, to use infrared- and fluorescence-based techniques to interrogate protein folding and functional dynamics. Specifically, we focus on discussing how to use extrinsic spectroscopic probes to enhance the structural resolution of these techniques and how to exploit various cross-linking strategies to acquire dynamic and mechanistic information that was previously difficult to attain.