Abstract
Abstract Protein-nucleic acid interactions involve intermolecular ion pairs of protein side-chain and DNA or RNA phosphate groups. Using three protein-DNA complexes, we demonstrate that site-specific oxygen-to-sulfur substitution in phosphate groups allows for identification of NMR signals from the protein side-chain NH3 + groups forming the intermolecular ion pairs. A characteristic change in their 1H and 15N resonances upon this modification (i.e., substitution of phosphate to phosphorodithioate) can represent a signature of an intermolecular ion pair. Hydrogen-bond scalar coupling between protein side-chain 15N and DNA phosphorodithiaote 31P nuclei provides direct confirmation of the intermolecular ion pair. The same approach is likely applicable to protein-RNA complexes as well.
Original language | English (US) |
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Article number | 9909 |
Pages (from-to) | 1-5 |
Number of pages | 5 |
Journal | Journal of Biomolecular NMR |
Volume | 62 |
Issue number | 1 |
DOIs | |
State | Published - Jun 1 2015 |
Keywords
- Hydrogen bonds
- Ion pairs
- NH groups
- Protein side chains
- Protein-nucleic acid interactions
ASJC Scopus subject areas
- Biochemistry
- Spectroscopy