Calculating proton uptake/release and binding free energy taking into account ionization and conformation changes induced by protein-inhibitor association application to plasmepsin, cathepsin D and endothiapepsin-pepstatin complexes

Proteins: Structure, Function and Genetics

Volumn 56, Issue 3, 2004, Pages 572-584

  Alexov, Emil ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

Binding free energy; Conformation changes; DelPhi; Multi Conformation Continuum Electrostatics (MCCE); pH dependence; Poisson Boltzmann; Protein ligand binding; Protein protein interactions; Proton uptake release

Indexed keywords

CATHEPSIN D; ENDOTHIAPEPSIN; PEPSTATIN; PLASMEPSIN I;

ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; ELECTRICITY; ENERGY; ENZYME ACTIVE SITE; HUMAN; IONIZATION; MATHEMATICAL ANALYSIS; MOLECULAR MODEL; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; PROTON TRANSPORT;

AMINO ACID SEQUENCE; ASPARTIC ENDOPEPTIDASES; BINDING SITES; CALORIMETRY; CATHEPSIN D; ELECTROSTATICS; HYDROGEN-ION CONCENTRATION; IONS; MODELS, CHEMICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPSTATINS; PEPTIDE HYDROLASES; PROTEASE INHIBITORS; PROTEIN BINDING; PROTEIN CONFORMATION; PROTONS; SEQUENCE HOMOLOGY, AMINO ACID; THERMODYNAMICS;

EID: 3142708566     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.20107     Document Type: Article

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