Fetler, L <br/><br/>
Unlike the quaternary structure transition, the tertiary structure change of the 240s loop in allosteric aspartate transcarbamylase requires active site saturation by substrate for completion.  [electronic resource] 

 -  Biochemistry  Dec 1995 
 - 15654-60 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi00048a008  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Allosteric Site<br/>Aspartate Carbamoyltransferase--chemistry<br/>Binding Sites<br/>Escherichia coli--enzymology<br/>Fluorescent Dyes<br/>Protein Structure, Secondary<br/>Scattering, Radiation<br/>Spectrometry, Fluorescence<br/>Substrate Specificity<br/>X-Rays