Quantum mechanical modeling of aspartic proteinase interactions: Difference in binding of diastereomeric statine models
- 1 December 1988
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 157 (2) , 450-456
- https://doi.org/10.1016/s0006-291x(88)80270-5
Abstract
No abstract availableThis publication has 15 references indexed in Scilit:
- Statine and its derivatives. Conformational studies using nuclear magnetic resonance spectrometry and energy calculationsInternational Journal of Peptide and Protein Research, 2009
- Theoretical calculations on the acidity of the active site in aspartic proteinasesBiochemistry, 1988
- Conformational preferences and self‐association modes of two diastereomeric statine derivativesInternational Journal of Peptide and Protein Research, 1987
- On the rational design of renin inhibitors: x-ray studies of aspartic proteinases complexed with transition-state analogsBiochemistry, 1987
- Improvement of the hydrogen bonding correction to MNDO for calculations of biochemical interestJournal of Computational Chemistry, 1987
- Three-dimensional structure of the complex of the Rhizopus chinensis carboxyl proteinase and pepstatin at 2.5 .ANG. resolutionBiochemistry, 1982
- Synthesis of analogs of the carboxyl protease inhibitor pepstatin. Effect of structure on inhibition of pepsin and reninJournal of Medicinal Chemistry, 1980
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977
- The effect of arginine modification on the pH dependence of pepsin activityFEBS Letters, 1971
- PEPSTATIN, A NEW PEPSIN INHIBITOR PRODUCED BY AGTINOMYGETESThe Journal of Antibiotics, 1970