title: Structural thermodynamic study of the binding of renin inhibitors to endothiapepsin.
authors.affiliation: Department of Biology and the Biocalorimetry Center, Johns Hopkins University, Baltimore, Maryland 21218, USA.
authors.forename: J
authors.initials: J
authors.lastname: Gómez
authors.forename: N
authors.initials: N
authors.lastname: Semo
authors.forename: E
authors.initials: E
authors.lastname: Freire
mesh_terms: D000808:Angiotensinogen / Q000031:analogs & derivatives / Q000378:metabolism; D016282:Aspartic Acid Endopeptidases / Q000378:metabolism*; D009842:Oligopeptides / Q000378:metabolism; D011480:Protease Inhibitors / Q000378:metabolism*; D013329:Structure-Activity Relationship; D013816:Thermodynamics; D000092502:Renin Inhibitors
chemical_list: D000808:Angiotensinogen; D016282:Aspartic Acid Endopeptidases; D009842:Oligopeptides; D011480:Protease Inhibitors; D000092502:Renin Inhibitors; C034503:H 77; C039583:H 142; C045142:H 189; C046598:H 261; C042466:Endothia aspartic proteinase