Site-directed fluorescence approaches to monitor the structural dynamics of proteins using intrinsic Trp and labeled with extrinsic fluorophores

被引：16

作者：

Brahma, Rupasree ^{[1
]}

Das, Anindita ^{[1
]}

Raghuraman, H. ^{[1
]}

机构：

[1] CI Homi Bhabha Natl Inst, Saha Inst Nucl Phys, Crystallog & Mol Biol Div, 1-AF Bidhannagar, Kolkata 700064, India

来源：

STAR PROTOCOLS | 2022年 / 3卷 / 01期

基金：

英国惠康基金;

关键词：

IONIC-STRENGTH; MELITTIN; ORGANIZATION; CHOLESTEROL; TRANSITIONS; MECHANISMS; CHANNEL; CONFORMATIONS; MEMBRANES; PEPTIDE;

D O I：

10.1016/j.xpro.2022.101200

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Comprehensive understanding of a protein's function depends on having reliable, sophisticated tools to study protein structural dynamics in physiologically-relevant conditions. Here, we present an effective, robust step- by- step protocol to monitor the structural dynamics ( including hydration dynamics) of a protein utilizing various site-directed fluorescence (SDFL) approaches. This protocol should be widely applicable for studying soluble proteins, intrinsically-disordered proteins, and membrane proteins. For complete details on the use and execution of this protocol, please refer to Das et al. (2020), Das and Raghuraman (2021), and Chatterjee et al. (2021).

引用

页数：30

共 68 条

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