Protein Side-Chain–DNA Contacts Probed by Fast Magic-Angle Spinning NMR
Author:
Affiliation:
1. Physical Chemistry, ETH Zurich, 8093 Zurich, Switzerland
2. Institute of Molecular Biology and Biophysics, ETH Zurich, 8093 Zurich, Switzerland
3. Institute of Biochemistry, ETH Zurich, 8093 Zurich, Switzerland
Funder
Eidgen?ssische Technische Hochschule Z?rich
Schweizerischer Nationalfonds zur F?rderung der Wissenschaftlichen Forschung
H2020 Marie Sklodowska-Curie Actions
H2020 European Research Council
Publisher
American Chemical Society (ACS)
Subject
Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry
Link
http://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.0c08150
Reference69 articles.
1. Noncovalent interactions
2. Protein-nucleic acid recognition: Statistical analysis of atomic interactions and influence of DNA structure
3. Direct Observation of the Ion-Pair Dynamics at a Protein–DNA Interface by NMR Spectroscopy
4. DNA–protein π-interactions in nature: abundance, structure, composition and strength of contacts between aromatic amino acids and DNA nucleobases or deoxyribose sugar
5. Amino acid-base interactions: a three-dimensional analysis of protein-DNA interactions at an atomic level
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