title: [Mechanism of action of aspartic proteases. IV.Conformational characteristics of a substrate and an inhibitor of rhizopuspepsin ].
abstract: On the basis of theoretical conformational analysis of separate peptide fragments, the conformational characteristics of two substrates and a substrate-like inhibitor of aspartic protease rhizopuspepsin were studied. It was shown that the spatial structure of these molecules is described by several families of conformations, the transition between which does not require the overcoming of high energy barriers. It was assumed that the stabilization of beta-structural conformations experimentally observed in inhibitor complexes is due to the greater predisposition of extended structures to the formation of effective intermolecular contacts with amino acid residues of the active site of the enzyme.
authors.affiliation: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia. ilko@enzyme.siobc.ras.ru
authors.forename: I V
authors.initials: IV
authors.lastname: Kashparov
authors.forename: M E
authors.initials: ME
authors.lastname: Popov
authors.forename: E M
authors.initials: EM
authors.lastname: Popov
mesh_terms: D016282:Aspartic Acid Endopeptidases / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D010446:Peptide Fragments / Q000737:chemistry; D011480:Protease Inhibitors / Q000737:chemistry*; D011487:Protein Conformation; D013379:Substrate Specificity
chemical_list: D010446:Peptide Fragments; D011480:Protease Inhibitors; D016282:Aspartic Acid Endopeptidases; C035794:rhizopuspepsin