Thermodynamic interpretation of protein dynamics from NMR relaxation measurements |
| |
Authors: | Spyracopoulos Leo |
| |
Institution: | Department 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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|