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 relax...

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Bibliographic Details
Published inProtein and peptide letters Vol. 12; no. 3; p. 235
Main Author Spyracopoulos, Leo
Format Journal Article
LanguageEnglish
Published Netherlands 01.04.2005
Subjects
Ligands
Models, Theoretical
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Protein Conformation
Proteins - chemistry
Proteins - metabolism
Temperature
Thermodynamics
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Summary: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.
ISSN:0929-8665
DOI:10.2174/0929866053587075