Tanner, J J <br/><br/>
Determinants of enzyme thermostability observed in the molecular structure of Thermus aquaticus D-glyceraldehyde-3-phosphate dehydrogenase at 25 Angstroms Resolution.  [electronic resource] 

 -  Biochemistry  Feb 1996 
 - 2597-609 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi951988q  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Binding Sites<br/>Crystallography, X-Ray<br/>Electrochemistry<br/>Enzyme Stability<br/>Glyceraldehyde-3-Phosphate Dehydrogenases--chemistry<br/>Hydrogen Bonding<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Molecular Structure<br/>Protein Conformation<br/>Sequence Homology, Amino Acid<br/>Thermodynamics<br/>Thermus--enzymology