Hennecke, J <br/><br/>
Random circular permutation of DsbA reveals segments that are essential for protein folding and stability.  [electronic resource] 

 -  Journal of molecular biology  Mar 1999 
 - 1197-215 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1006/jmbi.1998.2531  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Catalysis<br/>Endopeptidase K--metabolism<br/>Escherichia coli--enzymology<br/>Models, Molecular<br/>Oxidation-Reduction<br/>Protein Conformation<br/>Protein Denaturation<br/>Protein Disulfide-Isomerases--chemistry<br/>Protein Folding<br/>Protein Structure, Secondary<br/>Recombinant Fusion Proteins--chemistry<br/>Urea--chemistry