Russ. J. Bioorganic Chem., 1997, 23(10):706-717

The secondary structure of binase in solution determined by1H NMR

Nearly all resonances were assigned in the two-dimensional1H 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 in2H2O at pH 6.7 and 30°C. Coupling constants3J 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. © 1997 MAEe cyrillic signK Hayκa/Interperiodica Publishing.

Reibarkh MY, Nolde DE, Bocharov EV, Vasileva LI, Shulga AA, Kirpichnikov MP, Arseniev AS

IBCH: 5760
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