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

Overview

abstract

  • 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).

publication date

  • February 28, 2022

Research

keywords

  • Intrinsically Disordered Proteins

Identity

PubMed Central ID

  • PMC8889417

Scopus Document Identifier

  • 85125364083

Digital Object Identifier (DOI)

  • 10.1016/j.xpro.2022.101200

PubMed ID

  • 35252885

Additional Document Info

volume

  • 3

issue

  • 1