Structure-activity relationships on the study of β-galactosidase folding/unfolding due to interactions with immobilization additives: Triton X-100 and ethanol. [electronic resource]
Producer: 20170410Description: 87-92 p. digitalISSN:- 1879-0003
- Bacillus -- enzymology
- Enzyme Stability -- drug effects
- Enzymes, Immobilized -- chemistry
- Ethanol -- chemistry
- Hydrogen-Ion Concentration
- Hydrolysis
- Models, Molecular
- Octoxynol -- chemistry
- Protein Conformation, alpha-Helical -- drug effects
- Protein Conformation, beta-Strand -- drug effects
- Protein Unfolding -- drug effects
- Structure-Activity Relationship
- Surface-Active Agents -- chemistry
- Temperature
- beta-Galactosidase -- chemistry
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Publication Type: Journal Article
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