Protein dynamics from NMR
Copyright policy )Protein dynamics from NMR
The past several years have seen the development of a significant number of new multidimensional NMR methods for the study of molecular dynamics spanning a wide range of time scales. Applications involving a large number of different biological systems have emerged and correlations with function have been established. Unique insights are obtained that are not available from structure alone, indicating the importance of dynamics studies for understanding function.Key words: NMR spin relaxation, protein dynamics, protein structure.
- University of Toronto Canada
Binding Sites, Magnetic Resonance Spectroscopy, Macromolecular Substances, Protein Conformation, Proteins, Enzymes, src Homology Domains, DNA-Binding Proteins, Solutions, Motion, Structure-Activity Relationship, Bacterial Proteins, Animals, Humans, Thermodynamics, Pliability, Signal Transduction, Protein Binding
Binding Sites, Magnetic Resonance Spectroscopy, Macromolecular Substances, Protein Conformation, Proteins, Enzymes, src Homology Domains, DNA-Binding Proteins, Solutions, Motion, Structure-Activity Relationship, Bacterial Proteins, Animals, Humans, Thermodynamics, Pliability, Signal Transduction, Protein Binding
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