Thermodynamic Interpretation of Protein Dynamics from NMR Relaxation Measurements
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.
Document Type: Review Article
Affiliations: Department of Biochemistry,University of Alberta, Edmonton, Alberta, Canada, T6G 2H7, Canada.
Publication date: 2005-04-01
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- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.