A quantum mechanical model of the hydration and acidity of the active site in aspartic proteases.
Structural Biochemistry Program, Frederick Biomedical Supercomputing Center, PRI/DynCorp, National Cancer Institute-Frederick Cancer Research and Development Center, MD 21702-1201, USA.
I A
IA
Topol
R E
RE
Cachau
S K
SK
Burt
J W
JW
Erickson
D000595:Amino Acid Sequence; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D002384:Catalysis; D018360:Crystallography, X-Ray; D004563:Electrochemistry; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D017354:Point Mutation; D011487:Protein Conformation; D011789:Quantum Theory; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D013816:Thermodynamics
D011994:Recombinant Proteins; D016282:Aspartic Acid Endopeptidases