Protein Thermostability: Mechanism and Control Through Protein Engineering
- 1 January 1988
- journal article
- Published by Taylor & Francis in Biocatalysis
- Vol. 1 (4) , 257-273
- https://doi.org/10.3109/10242428808998167
Abstract
No abstract availableKeywords
This publication has 53 references indexed in Scilit:
- Control of oligomeric enzyme thermostability by protein engineering.Proceedings of the National Academy of Sciences, 1987
- Life at High TemperaturesScience, 1985
- The Mechanism of Irreversible Enzyme Inactivation at 100°CScience, 1985
- Hydrogen-deuterium exchange studies on guanidinated pig heart lactate dehydrogenaseBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983
- Biochemistry and physiological role of methionine sulfoxide residues in proteinsArchives of Biochemistry and Biophysics, 1983
- On the three-dimensional structure and catalytic mechanism of triose phosphate isomerasePhilosophical Transactions of the Royal Society of London. B, Biological Sciences, 1981
- Thermal stability and protein structureBiochemistry, 1979
- Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilusNature, 1977
- Principles of protein–protein recognitionNature, 1975
- The Thermodynamics of Protein Denaturation. II. A Model of Reversible Denaturation and Interpretations Regarding the Stability of ChymotrypsinogenJournal of the American Chemical Society, 1964