Mobility of Histidine Side Chains Analyzed with 15N NMR Relaxation and Cross-Correlation Data: Insight into Zinc-Finger–DNA Interactions
Author:
Affiliation:
1. Department of Biochemistry and Molecular Biology, Sealy Center for Structural Biology and Molecular Biophysics, University of Texas Medical Branch, Galveston, Texas 77555-1068, United States
Funder
National Institute of General Medical Sciences
Welch Foundation
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.9b03132
Reference25 articles.
1. Fersht, A. R. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding; Macmillan, 1998; pp 128–131.
2. Direct Observation of the Ion-Pair Dynamics at a Protein–DNA Interface by NMR Spectroscopy
3. Changes in conformational dynamics of basic side chains upon protein–DNA association
4. Internal Motions of Basic Side Chains of the Antennapedia Homeodomain in the Free and DNA-Bound States
5. Stereospecific Effects of Oxygen-to-Sulfur Substitution in DNA Phosphate on Ion Pair Dynamics and Protein-DNA Affinity
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