Proteolytic enzymes: General features of their mode of action
- 1 January 1980
- journal article
- review article
- Published by Wiley in Recueil des Travaux Chimiques des Pays-Bas
- Vol. 99 (6) , 185-190
- https://doi.org/10.1002/recl.19800990601
Abstract
No abstract availableThis publication has 22 references indexed in Scilit:
- Protein structure refinement: Streptomyces griseus serine protease A at 1.8 Å resolutionJournal of Molecular Biology, 1979
- The accuracy of refined protein structures: comparison of two independently refined models of bovine trypsinActa Crystallographica Section B: Structural Science, Crystal Engineering and Materials, 1979
- Crystallography of liver alcohol dehydrogenase complexed with substratesJournal of Molecular Biology, 1978
- Structure of actinidin: Details of the polypeptide chain conformation and active site from an electron density map at 2·8 Å resolutionJournal of Molecular Biology, 1977
- A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substratesJournal of Molecular Biology, 1977
- Mechanism of acid protease catalysis based on the crystal structure of penicillopepsinNature, 1977
- Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilusNature, 1977
- The refined crystal structure of bovine β-trypsin at 1·8 Å resolutionJournal of Molecular Biology, 1975
- An estimate of intraproteic electrostatic fields values originated by the peptide groups in α-ChymotrypsinBiochemical and Biophysical Research Communications, 1972
- A New Enzyme Containing a Synthetically Formed Active Site. Thiol-Subtilisin1Journal of the American Chemical Society, 1966