期刊
CURRENT OPINION IN BIOMEDICAL ENGINEERING
卷 12, 期 -, 页码 8-17出版社
ELSEVIER
DOI: 10.1016/j.cobme.2019.08.007
关键词
Protein conformational dynamics; Allostery; Molecular machines; Single-molecule FRET; Fluorescence correlation spectroscopy
资金
- European Research Council (ERC) under the European Union [742637]
- Planning and Budgeting Committee of the Council for Higher Education of Israel
- European Research Council (ERC) [742637] Funding Source: European Research Council (ERC)
Feynman commented that Everything that living things do can be understood in terms of the jiggling and wiggling of atoms. Proteins can jiggle and wiggle large structural elements such as domains and subunits as part of their functional cycles. Single-molecule fluorescence resonance energy transfer (smFRET) is an excellent tool to study conformational dynamics and decipher coordinated large-scale motions within proteins. smFRET methods introduced in recent years are geared toward understanding the time scales and amplitudes of function-related motions. This review discusses the methodology for obtaining and analyzing smFRET temporal trajectories that provide direct dynamic information on transitions between conformational states. It also introduces correlation methods that are useful for characterizing intramolecular motions. This arsenal of techniques has been used to study multiple molecular systems, from membrane proteins through molecular chaperones, and we examine some of these studies here. Recent exciting methodological novelties permit revealing very fast, submillisecond dynamics, whose relevance to protein function is yet to be fully grasped.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据