Thermodynamic interpretation of protein dynamics from NMR relaxation measurements.
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.
Spyracopoulos
Leo
L
Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7, Canada. leo.spyracopoulos@ualberta.ca
D008024:Ligands; D008962:Models, Theoretical; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics
D008024:Ligands; D011506:Proteins