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Thermodynamic Interpretation of Protein Dynamics from NMR Relaxation Measurements

[ Vol. 12 , Issue. 3 ]

Author(s):

Leo Spyracopoulos   Pages 235 - 240 ( 6 )

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.

Keywords:

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

Affiliation:

Department of Biochemistry,University of Alberta, Edmonton, Alberta, Canada, T6G 2H7, Canada.



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