A neutron laue diffraction study of endothiapepsin: Implications for the aspartic proteinase mechanism

Biochemistry

Volumn 40, Issue 44, 2001, Pages 13149-13157

  Coates, L ^a   Erskine, P T ^a   Wood, S P ^a   Myles, D A A ^b   Cooper, J B ^a  

^a UNIVERSITY OF SOUTHAMPTON   (United Kingdom)

^b INSTITUT LAUE LANGEVIN   (France)

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE BONDS;

AMINO ACIDS; CATALYSIS; FUNGI; NEUTRON DIFFRACTION; NEUTRONS; PH; PROTONS; X RAY CRYSTALLOGRAPHY;

ENZYMES;

ASPARTIC ACID; ASPARTIC PROTEINASE; ASPARTIC PROTEINASE INHIBITOR; CARBOXYLIC ACID DERIVATIVE; DEUTERIUM OXIDE; ENDOTHIAPEPSIN; FUNCTIONAL GROUP; FUNGAL ENZYME; HYDROGEN; LIGAND; NITROGEN; OLIGOPEPTIDE; PROTEINASE; PROTON;

ARTICLE; BETA SHEET; CATALYSIS; CHEMICAL BOND; CRYSTAL STRUCTURE; DIFFRACTION; ENZYME ACTIVE SITE; ENZYME INHIBITOR COMPLEX; ENZYME MECHANISM; IONIZATION; NEUTRON DIFFRACTION; PH; PRIORITY JOURNAL; PROTEIN STRUCTURE; PROTON TRANSPORT; X RAY CRYSTALLOGRAPHY;

ASPARTIC ACID; ASPARTIC ENDOPEPTIDASES; BINDING SITES; CRYSTALLOGRAPHY; MOLECULAR STRUCTURE; NEUTRONS; OLIGOPEPTIDES; PROTEASE INHIBITORS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTONS; X-RAY DIFFRACTION;

FUNGI;

EID: 0035818441     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi010626h     Document Type: Article

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