Campus Units

Chemistry, Biochemistry, Biophysics and Molecular Biology, Roy J. Carver Department of

Document Type

Article

Publication Version

Accepted Manuscript

Publication Date

4-19-2021

Journal or Book Title

Journal of Visualized Experiments

Volume

170

First Page

e62395

DOI

10.3791/62395

Abstract

Protein conformational dynamics play fundamental roles in regulation of enzymatic catalysis, ligand binding, allostery, and signaling, which are important biological processes. Understanding how the balance between structure and dynamics governs biological function is a new frontier in modern structural biology and has ignited several technical and methodological developments. Among these, CPMG relaxation dispersion solution NMR methods provide unique, atomic-resolution information on the structure, kinetics, and thermodynamics of protein conformational equilibria occurring on the µs-ms timescale. Here, the study presents detailed protocols for acquisition and analysis of a 15N relaxation dispersion experiment. As an example, the pipeline for the analysis of the µs-ms dynamics in the C-terminal domain of bacteria Enzyme I is shown.

Comments

This is a manuscript of an article published as Singh, Aayushi, Jeffrey A. Purslow, and Vincenzo Venditti. "15N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale." Journal of Visualized Experiments 170 (2021): e62395. DOI: 10.3791/62395. Posted with permission.

Copyright Owner

MyJove Corporation

Language

en

File Format

application/pdf

Available for download on Wednesday, April 19, 2023

Published Version

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