Structure-based prediction of binding affinities and molecular design of peptide ligands.
Luque
I
I
Department of Biology, Johns Hopkins University, Baltimore, Maryland 21218, USA.
Freire
E
E
D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000378:metabolism; D015195:Drug Design; D005544:Forecasting; D017320:HIV Protease Inhibitors / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D008024:Ligands; D008956:Models, Chemical; D008958:Models, Molecular; D009842:Oligopeptides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D010436:Pepstatins / Q000737:chemistry / Q000378:metabolism; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology; D011485:Protein Binding; D013816:Thermodynamics
D017320:HIV Protease Inhibitors; D008024:Ligands; D009842:Oligopeptides; D010436:Pepstatins; D010455:Peptides; C014195:Streptomyces pepsin inhibitor; D016282:Aspartic Acid Endopeptidases; C042466:Endothia aspartic proteinase; C031375:pepstatin