Prediction and analysis of structure, stability and unfolding of thermolysin-like proteases
- 1 August 1993
- journal article
- research article
- Published by Springer Nature in Journal of Computer-Aided Molecular Design
- Vol. 7 (4), 367-396
- https://doi.org/10.1007/bf02337558
Abstract
No abstract availableKeywords
This publication has 100 references indexed in Scilit:
- Energetic contribution of solvent-exposed ion pairs to alpha-helix structureJournal of Molecular Biology, 1992
- Analysis and modulation of protein stabilityCurrent Opinion in Biotechnology, 1991
- Surface electrostatic interactions contribute little to stability of barnaseJournal of Molecular Biology, 1991
- Construction of side-chains in homology modellingJournal of Molecular Biology, 1989
- Engineering protein thermal stability: Sequence statistics point to residue substitutions in α-helicesJournal of Molecular Biology, 1989
- Crystal structure of neutral protease from Bacillus cereus refined at 3.0A˚resolution and comparison with the homologous but more thermostable enzyme thermolysinJournal of Molecular Biology, 1988
- Ribbon models of macromoleculesJournal of Molecular Graphics, 1987
- Interactive program for visualization and modelling of proteins, nucleic acids and small moleculesJournal of Molecular Graphics, 1986
- How different amino acid sequences determine similar protein structures: The structure and evolutionary dynamics of the globinsJournal of Molecular Biology, 1980
- The protein data bank: A computer-based archival file for macromolecular structuresJournal of Molecular Biology, 1977