Thermodynamic Interpretation of Protein Dynamics from NMR Relaxation Measurements

Title: Thermodynamic Interpretation of Protein Dynamics from NMR Relaxation Measurements

Volume: 12 Issue: 3

Author(s): Leo Spyracopoulos

Affiliation:

Keywords: protein backbone and side chain dynamics, thermodynamics, nmr spin relaxation

Abstract: Protein dynamics and thermodynamics can be characterized through measurements of relaxation rates of side chain 2H and 13C, and backbone 15N 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.

Cite this article as:

Spyracopoulos Leo, Thermodynamic Interpretation of Protein Dynamics from NMR Relaxation Measurements, Protein & Peptide Letters 2005; 12 (3) . https://dx.doi.org/10.2174/0929866053587075

DOI https://dx.doi.org/10.2174/0929866053587075	Print ISSN 0929-8665
Publisher Name Bentham Science Publisher	Online ISSN 1875-5305