Open Access<sup>15</sup>N CPMG Relaxation Dispersion for the Investigation of Protein Conformational Dynamics on the µs-ms Timescale
Author(s) -
Aayushi Singh,
Jeffrey A. Purslow,
Vincenzo Venditti
Publication year - 2021
Publication title -
journal of visualized experiments
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.596
H-Index - 91
ISSN - 1940-087X
DOI - 10.3791/62395
Subject(s) - protein dynamics , relaxation (psychology) , allosteric regulation , chemistry , dynamics (music) , molecular dynamics , conformational change , kinetics , dispersion (optics) , biophysics , chemical physics , computational chemistry , physics , enzyme , stereochemistry , biochemistry , biology , quantum mechanics , neuroscience , acoustics , optics
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 15 N 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.