A chemical approach for site-specific identification of NMR signals from protein side-chain NH3 (+) groups forming intermolecular ion pairs in protein-nucleic acid complexes

作者：Anderson Kurtis M; Nguyen Dan; Esadze Alexandre; Zandrashvili Levani; Gorenstein David G; Iwahara Junji^*

来源：Journal of Biomolecular NMR, 2015, 62(1): 1-5.

DOI：10.1007/s10858-015-9909-8

• Protein-nucleic acid interactions
• Protein side chains
• NH3+ groups
• Ion pairs
• Hydrogen bonds

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 H-1 and N-15 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 N-15 and DNA phosphorodithiaote P-31 nuclei provides direct confirmation of the intermolecular ion pair. The same approach is likely applicable to protein-RNA complexes as well.

• 出版日期2015-5