Nandi, Sandip K <br/><br/>
A S52P mutation in the 'α-crystallin domain' of Mycobacterium leprae HSP18 reduces its oligomeric size and chaperone function.  [electronic resource] 

 -  The FEBS journal  Dec 2013 
 - 5994-6009 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>1742-4658 
<br/><br/><label>Standard No.: </label>10.1111/febs.12519  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Bacterial Proteins--chemistry<br/>Heat-Shock Proteins--chemistry<br/>Molecular Chaperones--metabolism<br/>Molecular Sequence Data<br/>Mutagenesis, Site-Directed<br/>Mutant Proteins--chemistry<br/>Mutation--genetics<br/>Mycobacterium leprae<br/>Protein Folding<br/>Protein Multimerization<br/>Sequence Homology, Amino Acid<br/>alpha-Crystallins--genetics