Do Globular Proteins Require Some Structural Peculiarity To Best Function at High Temperatures?
- 1 January 1995
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 117 (1) , 16-20
- https://doi.org/10.1021/ja00106a002
Abstract
No abstract availableThis publication has 13 references indexed in Scilit:
- Heat capacity of proteinsJournal of Molecular Biology, 1990
- Common Features of Protein Unfolding and Dissolution of Hydrophobic CompoundsScience, 1990
- Large increases in general stability for subtilisin BPN' through incremental changes in the free energy of unfoldingBiochemistry, 1989
- Conformational stability and mechanism of folding of ribonuclease T1Journal of Biological Chemistry, 1989
- Protein stability curvesBiopolymers, 1987
- Interior and surface of monomeric proteinsJournal of Molecular Biology, 1987
- Temperature dependence of the hydrophobic interaction in protein folding.Proceedings of the National Academy of Sciences, 1986
- PROTEIN THERMOSTABILITY - CORRELATIONS BETWEEN CALCULATED MACROSCOPIC PARAMETERS AND GROWTH TEMPERATURE FOR CLOSELY RELATED THERMOPHILIC AND MESOPHILIC BACILLI1981
- TIGHT PACKING OF PROTEIN CORES AND INTERFACES - RELATION TO CONSERVATIVE AMINO-ACID SEQUENCES AND STABILITY OF PROTEIN-PROTEIN INTERACTION1978
- Reversible thermal unfolding of thermostable phosphoglycerate kinase. Thermostability associated with mean zero enthalpy changeJournal of Molecular Biology, 1977