Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for nonequivalent binding surfaces on the chaperonin molecule. [electronic resource]
Producer: 19960117Description: 28126-32 p. digitalISSN:- 0021-9258
- 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
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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