Dohnálek, Jan <br/><br/>
Hydroxyethylamine isostere of an HIV-1 protease inhibitor prefers its amine to the hydroxy group in binding to catalytic aspartates. A synchrotron study of HIV-1 protease in complex with a peptidomimetic inhibitor.  [electronic resource] 

 -  Journal of medicinal chemistry  Mar 2002 
 - 1432-8 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-2623 
<br/><br/><label>Standard No.: </label>10.1021/jm010979e  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amines--chemistry<br/>Amino Acids--chemistry<br/>Aspartic Acid--chemistry<br/>Binding Sites<br/>Catalysis<br/>Dimerization<br/>Endopeptidases--chemistry<br/>Ethanolamines--chemistry<br/>Glycerol--chemistry<br/>HIV Protease--metabolism<br/>HIV Protease Inhibitors--chemistry<br/>Hydrogen Bonding<br/>Kinetics<br/>Models, Chemical<br/>Models, Molecular<br/>Oxygen--chemistry<br/>Peptide Fragments<br/>Protein Binding<br/>Protein Conformation<br/>Synchrotrons<br/>X-Ray Diffraction