The secondary structure of binase in solution determined by 1H NMR

M. Ya Reibarkh, D. E. Nolde, E. V. Bocharov, L. I. Vasil'eva, A. A. Shulga, M. P. Kirpichnikov, A. S. Arseniev

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)

Abstract

Nearly all resonances were assigned in the two-dimensional 1H NMR spectra of binase, guanylospecific ribonuclease from Bacillus intermedius containing 109 amino acid residues. The exchange rates of amide protons with solvent deuterium were measured in 2H2O at pH 6.7 and 30°C. Coupling constants 3J of H-NCα-H, NOE contacts, solvent exchange rates of amide protons, and indices of CαH chemical shifts were measured, and the binase secondary structure was deduced from these data. It involves three α-helices in the N-terminal part (the 6-16, 26-31, and 41-45 segments) and a β-sheet formed by five antiparallel β-strands (51-55, 71-75, 86-90, 95-99, and 104-108 segments). The binase secondary structure was compared with that of its closest homologue, barnase from B. amyloliquefaciens.

Original languageEnglish
Pages (from-to)706-717
Number of pages12
JournalRussian Journal of Bioorganic Chemistry
Volume23
Issue number10
Publication statusPublished - Oct 1997
Externally publishedYes

Keywords

  • NMR
  • Proteins
  • Ribonucleases
  • Secondary structure

ASJC Scopus subject areas

  • Biochemistry
  • Organic Chemistry

Fingerprint Dive into the research topics of 'The secondary structure of binase in solution determined by <sup>1</sup>H NMR'. Together they form a unique fingerprint.

Cite this