Related Experiment Video
Updated: May 7, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Monitoring side-chain dynamics of proteins using (2)H relaxation
1Division of Chemical Biology and Medicinal Chemistry, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA.
Abstract:
Nuclear magnetic resonance (NMR) is a powerful technique capable of monitoring a wide range of motions in proteins on a per residue basis. A variety of (2)H relaxation experiments have been developed for monitoring side-chain methyl group motions on the picosecond-nanosecond timescale. These experiments enable determination of the order parameter, S (2) axis, which reports on the rigidity of the C-CH3 bond for side-chain methyl groups. The application of a commonly used subset of these experiments is described in this chapter. It is intended to serve as a practical guide to investigators interested in monitoring side-chain motions.
More Related Videos
Related Concept Videos
Protein Dynamics in Living Cells
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...
Atomic Nuclei: Types of Nuclear Relaxation
In spin–lattice or longitudinal relaxation, the excited spins exchange energy with the surrounding lattice as they return to the lower energy level. Among several mechanisms that contribute to spin–lattice relaxation, magnetic dipolar interactions are significant. Here, the excited nucleus transfers energy to a nearby...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
Two-Dimensional (2D) NMR: Overview
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.

