Ginsburg, A <br/><br/>
Conformational stability changes of the amino terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate: sugar phosphotransferase system produced by substituting alanine or glutamate for the active-site histidine 189: implications for phosphorylation effects.  [electronic resource] 

 -  Protein science : a publication of the Protein Society  Jun 2000 
 - 1085-94 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0961-8368 
<br/><br/><label>Standard No.: </label>10.1110/ps.9.6.1085  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Alanine--chemistry<br/>Amino Acid Substitution<br/>Binding Sites<br/>Calorimetry, Differential Scanning<br/>Escherichia coli--enzymology<br/>Glutamic Acid--chemistry<br/>Histidine--chemistry<br/>Models, Molecular<br/>Phosphoenolpyruvate Sugar Phosphotransferase System--chemistry<br/>Phosphorylation<br/>Phosphotransferases (Nitrogenous Group Acceptor)--chemistry<br/>Protein Conformation<br/>Protein Denaturation<br/>Thermodynamics