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

Autor:	Kurtis M, Anderson, Dan, Nguyen, Alexandre, Esadze, Levani, Zandrashvili, David G, Gorenstein, Junji, Iwahara
Rok vydání:	2014
Předmět:	Models Molecular Proteins RNA Hydrogen Bonding DNA Nuclear Magnetic Resonance Biomolecular Article
Zdroj:	Journal of biomolecular NMR. 62(1)
ISSN:	1573-5001
Popis:	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 (1)H and (15)N 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 (15)N and DNA phosphorodithiaote (31)P nuclei provides direct confirmation of the intermolecular ion pair. The same approach is likely applicable to protein-RNA complexes as well.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::1890488cae9ffbc7aa9a828979b2b203 https://pubmed.ncbi.nlm.nih.gov/25690740 Zobrazit plný text záznamu Full text from SpringerLink