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荧光各向异性和共振能量转移:在生理环境中实时测量蛋白质动力学的有力工具。

Fluorescence anisotropy and resonance energy transfer: powerful tools for measuring real time protein dynamics in a physiological environment.

机构信息

Department of Cellular and Molecular Physiology, College of Medicine, Pennsylvania State University, Hershey, PA 17033, USA.

出版信息

Curr Opin Pharmacol. 2010 Dec;10(6):731-7. doi: 10.1016/j.coph.2010.09.013. Epub 2010 Oct 23.

DOI:10.1016/j.coph.2010.09.013
PMID:20971683
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2981669/
Abstract

Fluorescence spectroscopy/microscopy is a versatile method for examining protein dynamics in vitro and in vivo that can be combined with other techniques to simultaneously examine complementary pharmacological parameters. The following review will highlight the advantages and challenges of using fluorescence spectroscopic methods for examining protein dynamics with a special emphasis on fluorescence resonance energy transfer and fluorescence anisotropy. Both of these methods are amenable to measurements on an ensemble of molecules as well as at the single molecule level, in live cells and in high throughput screening assays, providing a powerful set of tools to aid in the design and testing of new drugs under a variety of experimental conditions.

摘要

荧光光谱/显微镜是一种用于体外和体内研究蛋白质动力学的多功能方法,它可以与其他技术结合使用,同时检查互补的药理学参数。本综述将重点介绍使用荧光光谱方法研究蛋白质动力学的优点和挑战,特别强调荧光共振能量转移和荧光各向异性。这两种方法都适用于对分子集合以及单个分子进行测量,适用于活细胞和高通量筛选测定,为在各种实验条件下设计和测试新药提供了一套强大的工具。

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Surfing on a new wave of single-molecule fluorescence methods.冲浪于单分子荧光方法的新浪潮之上。
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Using Three-color Single-molecule FRET to Study the Correlation of Protein Interactions.使用三色单分子荧光共振能量转移技术研究蛋白质相互作用的相关性。
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