Premium
Assignment of resonances of exchangeable protons in the NMR spectrum of the complex formed by Escherichia coli ribosomal protein L25 and uniformly nitrogen‐15 enriched 5 S RNA fragment
Author(s) -
Kime Matthew J.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80747-4
Subject(s) - nucleic acid , chemistry , rna , guanine , chemical shift , escherichia coli , uracil , proton , nuclear magnetic resonance spectroscopy , crystallography , stereochemistry , dna , biochemistry , nucleotide , physics , quantum mechanics , gene
The downfield proton NMR spectrum of the aqueous nucleoprotein complex formed by Escherichia coli ribosomal protein L25 and uniformly nitrogen‐15 enriched 5 S RNA fragment is presented. Many proton resonances show the effects of scalar coupling to nitrogen‐15 and these resonances arc assigned to nucleic acid imino protons. Selective nitrogen‐15 decoupling difference proton spectroscopy revealed nitrogen‐15 and proton chemical shift correlations from which the base types of nucleic acid imino proton resonances could be assigned because the nitrogen‐15 chemical shifts of nucleic acid guanine and uracil imino nitrogens have separate small ranges for both nucleoproteins and isolated nucleic acids.