费斯特共振能量转移
蛋白质动力学
功能(生物学)
生物物理学
蛋白质结构
分子动力学
化学
构象变化
单分子微动
蛋白质功能
核磁共振波谱
化学物理
生物系统
核磁共振
物理
荧光
计算化学
生物
生物化学
量子力学
进化生物学
基因
作者
Paul Schanda,Gilad Haran
标识
DOI:10.1146/annurev-biophys-070323-022428
摘要
Proteins often undergo large-scale conformational transitions, in which secondary and tertiary structure elements (loops, helices, and domains) change their structures or their positions with respect to each other. Simple considerations suggest that such dynamics should be relatively fast, but the functional cycles of many proteins are often relatively slow. Sophisticated experimental methods are starting to tackle this dichotomy and shed light on the contribution of large-scale conformational dynamics to protein function. In this review, we focus on the contribution of single-molecule Förster resonance energy transfer and nuclear magnetic resonance (NMR) spectroscopies to the study of conformational dynamics. We briefly describe the state of the art in each of each of these techniques and then point out their similarities and differences, as well as the relative strengths and weaknesses of each. Several case studies, in which the connection between fast conformational dynamics and slower function has been demonstrated, are then introduced and discussed. These examples include both enzymes and large protein machines, some of which have been studied by both NMR and fluorescence spectroscopies. Expected final online publication date for the Annual Review of Biophysics, Volume 53 is May 2024. Please see http://www.annualreviews.org/page/journal/pubdates for revised estimates.
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