NMR Observation of Intermolecular Hydrogen Bonds between Protein Tyrosine Side-Chain OH and DNA Phosphate Groups | Zendy

Binhan Yu | Zendy; Channing C. Pletka | Zendy; Junji Iwahara | Zendy

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NMR Observation of Intermolecular Hydrogen Bonds between Protein Tyrosine Side-Chain OH and DNA Phosphate Groups

Author(s) -

Binhan Yu,

Channing C. Pletka,

Junji Iwahara

Publication year - 2020

Publication title -

the journal of physical chemistry b

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.864

H-Index - 392

eISSN - 1520-6106

pISSN - 1520-5207

DOI - 10.1021/acs.jpcb.9b10987

Subject(s) - hydrogen bond , chemistry , intermolecular force , dna , side chain , phosphate , rna , crystallography , low barrier hydrogen bond , stereochemistry , biochemistry , molecule , organic chemistry , gene , polymer

Hydrogen bonds between protein side-chain hydroxyl (OH) and phosphate groups are one of the most common types of intermolecular hydrogen bonds in protein-DNA/RNA complexes. Using NMR spectroscopy, we identified and characterized the hydrogen bonds between tyrosine side-chain OH and DNA phosphate groups in a protein-DNA complex. These OH groups exhibited relatively slow hydrogen-exchange rates and sizable scalar couplings between hydroxyl 1 H and DNA phosphate 31 P nuclei across the hydrogen bonds. Information about intermolecular hydrogen bonds facilitates investigations of the DNA/RNA recognition by the protein.

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