Related Experiment Video
Updated: Aug 19, 2026

NMR 15N Relaxation Experiments for the Investigation of Picosecond to Nanoseconds Structural Dynamics of Proteins
Published on: November 1, 2024
Thermodynamic interpretation of protein dynamics from NMR relaxation measurements
1Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7, Canada. leo.spyracopoulos@ualberta.ca
Abstract:
Protein dynamics and thermodynamics can be characterized through measurements of relaxation rates of side chain (2)H and (13)C, and backbone (15)N nuclei using NMR spectroscopy. The rates reflect protein motions on timescales from picoseconds to milliseconds. Backbone and methyl side chain NMR relaxation measurements for several proteins are beginning to reveal the role of protein dynamics in protein stability and ligand binding.
Related Concept Videos
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...
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 Conformationally Flexible Molecules: Variable-Temperature NMR
Atomic Nuclei: Nuclear Spin State Population Distribution

