Privé, G G <br/><br/>
X-ray crystal structures of transforming p21 ras mutants suggest a transition-state stabilization mechanism for GTP hydrolysis.  [electronic resource] 

 -  Proceedings of the National Academy of Sciences of the United States of America  Apr 1992 
 - 3649-53 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>0027-8424 
<br/><br/><label>Standard No.: </label>10.1073/pnas.89.8.3649  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Binding Sites<br/>Guanosine Triphosphate--metabolism<br/>Humans<br/>Hydrolysis<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Mutation<br/>Protein Conformation<br/>Proto-Oncogene Proteins p21(ras)--chemistry<br/>X-Ray Diffraction--methods