Аннотация
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.
Язык оригинала | Английский |
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Страницы (с-по) | 794 |
Число страниц | 1 |
Журнал | Bioorganicheskaya Khimiya |
Том | 23 |
Номер выпуска | 10 |
Состояние | Опубликовано - 1997 |
Опубликовано для внешнего пользования | Да |
ASJC Scopus subject areas
- Medicine(all)