Smoot, A L <br/><br/>
The binding of bis-ANS to the isolated GroEL apical domain fragment induces the formation of a folding intermediate with increased hydrophobic surface not observed in tetradecameric GroEL.  [electronic resource] 

 -  Biochemistry  Apr 2001 
 - 4484-92 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi001822b  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Anilino Naphthalenesulfonates--metabolism<br/>Binding Sites<br/>Chaperonin 60--chemistry<br/>Circular Dichroism<br/>Fluorescent Dyes--metabolism<br/>Kinetics<br/>Peptide Fragments--chemistry<br/>Protein Binding<br/>Protein Denaturation<br/>Protein Folding<br/>Protein Structure, Tertiary<br/>Spectrometry, Fluorescence<br/>Surface Properties<br/>Tyrosine--chemistry<br/>Ultracentrifugation<br/>Urea--chemistry