Park, Y C <br/><br/>
Dimeric tyrosyl-tRNA synthetase from Bacillus stearothermophilus unfolds through a monomeric intermediate. A quantitative analysis under equilibrium conditions.  [electronic resource] 

 -  The Journal of biological chemistry  Jul 1998 
 - 18052-9 p.  digital 
<br/><br/> Publication Type: Journal Article 
<br/><br/><label>ISSN: </label>0021-9258 
<br/><br/><label>Standard No.: </label>10.1074/jbc.273.29.18052  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Chromatography, Gel<br/>Circular Dichroism<br/>Dimerization<br/>Diphosphates--metabolism<br/>Geobacillus stearothermophilus--enzymology<br/>Protein Conformation<br/>Protein Denaturation<br/>Protein Folding<br/>Spectrometry, Fluorescence<br/>Thermodynamics<br/>Tyrosine-tRNA Ligase--metabolism<br/>Urea