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

Abstract

Nearly all resonances were assigned in the two-dimensional 1H NMR spectra of binase, guanyl-ospecific ribonuclease from Bacillus intermedius containing 109 amino acid residues. The exchange rates of amide protons with the 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)794
Number of pages1
JournalBioorganicheskaya Khimiya
Volume23
Issue number10
Publication statusPublished - 1997
Externally publishedYes

Keywords

  • NMR
  • Proteins
  • Ribonucleases
  • Secondary structure

ASJC Scopus subject areas

  • Medicine(all)

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