Heat and SDS insensitive NDK dimers are largely stabilised by hydrophobic interaction to form functional hexamer in Mycobacterium smegmatis.
Arumugam, Muthu
Heat and SDS insensitive NDK dimers are largely stabilised by hydrophobic interaction to form functional hexamer in Mycobacterium smegmatis. [electronic resource] - Acta biochimica Polonica 2013 - 199-207 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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
Heat and SDS insensitive NDK dimers are largely stabilised by hydrophobic interaction to form functional hexamer in Mycobacterium smegmatis. [electronic resource] - Acta biochimica Polonica 2013 - 199-207 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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