Arumugam, Muthu <br/><br/>
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 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1734-154X 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Electrophoresis, Polyacrylamide Gel<br/>Hydrophobic and Hydrophilic Interactions<br/>Models, Molecular<br/>Mycobacterium smegmatis--enzymology<br/>Mycobacterium tuberculosis--enzymology<br/>Nucleoside-Diphosphate Kinase--chemistry<br/>Protein Multimerization--physiology<br/>Protein Structure, Quaternary<br/>Recombinant Proteins--chemistry<br/>Sodium Dodecyl Sulfate--pharmacology