Heat and SDS insensitive NDK dimers are largely stabilised by hydrophobic interaction to form functional hexamer in Mycobacterium smegmatis. [electronic resource]
Producer: 20131024Description: 199-207 p. digitalISSN:- 1734-154X
- Electrophoresis, Polyacrylamide Gel
- Hydrophobic and Hydrophilic Interactions
- Models, Molecular
- Mycobacterium smegmatis -- enzymology
- Mycobacterium tuberculosis -- enzymology
- Nucleoside-Diphosphate Kinase -- chemistry
- Protein Multimerization -- physiology
- Protein Structure, Quaternary
- Recombinant Proteins -- chemistry
- Sodium Dodecyl Sulfate -- pharmacology
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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