Related Experiment Video
Updated: Jun 6, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
An introduction to NMR-based approaches for measuring protein dynamics
Ian R Kleckner1, Mark P Foster
1The Ohio State University Biophysics Program, 484 West 12th Ave Room 776, Columbus, OH 43210, USA.
None:
Proteins are inherently flexible at ambient temperature. At equilibrium, they are characterized by a set of conformations that undergo continuous exchange within a hierarchy of spatial and temporal scales ranging from nanometers to micrometers and femtoseconds to hours. Dynamic properties of proteins are essential for describing the structural bases of their biological functions including catalysis, binding, regulation and cellular structure. Nuclear magnetic resonance (NMR) spectroscopy represents a powerful technique for measuring these essential features of proteins. Here we provide an introduction to NMR-based approaches for studying protein dynamics, highlighting eight distinct methods with recent examples, contextualized within a common experimental and analytical framework. The selected methods are (1) Real-time NMR, (2) Exchange spectroscopy, (3) Lineshape analysis, (4) CPMG relaxation dispersion, (5) Rotating frame relaxation dispersion, (6) Nuclear spin relaxation, (7) Residual dipolar coupling, (8) Paramagnetic relaxation enhancement. This article is part of a Special Issue entitled: Protein Dynamics: Experimental and Computational Approaches.
Related Concept Videos
Applications Of NMR In Biology
The...
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...
¹H NMR of Conformationally Flexible Molecules: Temporal Resolution
¹H NMR of Labile Protons: Temporal Resolution
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
Two-Dimensional (2D) NMR: Overview
The first step is the preparation period, during which nucleus A is excited with a radiofrequency pulse.
2D NMR: Overview of Heteronuclear Correlation Techniques

