1H, 13C and 15N NMR backbone assignments and secondary structure of the 269-residue protease subtilisin 309 from Bacillus lentus
- 1 March 1994
- journal article
- research article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 4 (2) , 257-278
- https://doi.org/10.1007/bf00175252
Abstract
No abstract availableKeywords
This publication has 23 references indexed in Scilit:
- Crystal structure of the alkaline proteinase Savinase™ from Bacillus lentus at 1.4 Å resolutionPublished by Elsevier ,2005
- Significance of hydrophobic S4-P4 interactions in subtilisin 309 from Bacillus lentusBiochemistry, 1993
- Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteinsJournal of Biomolecular NMR, 1993
- Proton, carbon-13, and nitrogen-15 NMR backbone assignments and secondary structure of human interferon-.gamma.Biochemistry, 1992
- Three‐dimensional structure of proteinase K at 0.15‐nm resolutionEuropean Journal of Biochemistry, 1988
- Nitrogen-15 NMR spectroscopy of the catalytic-triad histidine of a serine protease in peptide boronic acid inhibitor complexesBiochemistry, 1988
- X-ray crystallographic study of boronic acid adducts with subtilisin BPN' (Novo). A model for the catalytic transition state.Journal of Biological Chemistry, 1975
- High resolution nuclear magnetic resonance studies of the active site of chymotrypsin: II. Polarization of histidine 57 by substrate analogues and competitive inhibitorsJournal of Molecular Biology, 1974
- n‐Alkylboronic acids as bifunctional reversible inhibitors of α‐chymotrypsinFEBS Letters, 1970
- Structure of Subtilisin BPN′ at 2.5 Å ResolutionNature, 1969