Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule. [electronic resource]
- The Journal of biological chemistry Nov 1995
- 28126-32 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
0021-9258
10.1074/jbc.270.47.28126 doi
Alcohol Dehydrogenase--chemistry Animals Chaperonins--chemistry Chickens Egg White Enzymes--chemistry Female Hot Temperature Kinetics Liver--enzymology Macromolecular Substances Malate Dehydrogenase--chemistry Muramidase--chemistry Saccharomyces cerevisiae--enzymology Sulfolobus--metabolism Thermodynamics Time Factors alpha-Glucosidases--chemistry