Zhang, Aihua <br/><br/>
Productive interaction of chaperones with substrate protein domains allows correct folding of the downstream GFP domain.  [electronic resource] 

 -  Gene  Apr 2005 
 - 25-31 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0378-1119 
<br/><br/><label>Standard No.: </label>10.1016/j.gene.2005.01.019  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Substitution<br/>Animals<br/>Binding Sites--genetics<br/>Catalytic Domain--genetics<br/>Electrophoresis, Polyacrylamide Gel<br/>Escherichia coli Proteins--genetics<br/>Fluorescence<br/>Green Fluorescent Proteins--chemistry<br/>HSP70 Heat-Shock Proteins--genetics<br/>Molecular Chaperones--genetics<br/>Phosphoprotein Phosphatases--genetics<br/>Protein Binding<br/>Protein Folding<br/>Protein Structure, Tertiary<br/>Rabbits<br/>Recombinant Fusion Proteins--chemistry<br/>Solubility<br/>Spectrometry, Fluorescence<br/>Substrate Specificity