A 13C Labeling Strategy Reveals a Range of Aromatic Side Chain Motion in Calmodulin
Author:
Affiliation:
1. Graduate Group in Biochemistry and Molecular Biophysics and the Johnson Research Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania 19104, United States
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja4001129
Reference37 articles.
1. New Tools Provide New Insights in NMR Studies of Protein Dynamics
2. Fast Time Scale Dynamics of Protein Backbones: NMR Relaxation Methods, Applications, and Functional Consequences
3. Characterization of the Fast Dynamics of Protein Amino Acid Side Chains Using NMR Relaxation in Solution
4. The role of conformational entropy in molecular recognition by calmodulin
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