Loop-tryptophan human purine nucleoside phosphorylase reveals submillisecond protein dynamics

Biochemistry

Volumn 48, Issue 16, 2009, Pages 3658-3668

  Ghanem, Mahmoud ^a   Zhadin, Nickolay ^a   Callender, Robert ^a   Schramm, Vern L ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; BULK SOLVENTS; CATALYTIC SITES; CONFORMATIONAL DYNAMICS; CONFORMATIONAL EQUILIBRIUM; HOMOTRIMER; HYDROPHOBIC CLUSTERS; HYDROPHOBIC RESIDUES; LASER INDUCED; LIGAND BINDING; NOVEL PROTEINS; PROTEIN DYNAMICS; PURINE NUCLEOSIDE PHOSPHORYLASE; QM/MM CALCULATIONS; RED-SHIFTED; RELAXATION KINETICS; SUBUNIT INTERFACES; TEMPERATURE RANGE; TERNARY COMPLEX; THERMODYNAMIC EQUILIBRIUM CONSTANT; TIME-SCALE; TRANSITION STATE; TRYPTOPHAN RESIDUES;

AMINO ACIDS; CONFORMATIONS; DYNAMICS; EQUILIBRIUM CONSTANTS; FLUORESCENCE; HYDROPHOBICITY; LIGANDS; SUBSTRATES;

BINDING SITES;

HYPOXANTHINE; PURINE NUCLEOSIDE PHOSPHORYLASE; TRYPTOPHAN; FORODESINE; PROTEIN SUBUNIT; PURINE NUCLEOSIDE; PYRIMIDINONE DERIVATIVE;

ARTICLE; CATALYSIS; CRYSTAL STRUCTURE; ENTHALPY; ENZYME INHIBITION; EQUILIBRIUM CONSTANT; FLUORESCENCE; HYDROPHOBICITY; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; STEADY STATE; TEMPERATURE DEPENDENCE; THERMODYNAMICS; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVE SITE; GENETICS; HUMAN; KINETICS; METABOLISM; PROTEIN BINDING; SITE DIRECTED MUTAGENESIS;

CATALYTIC DOMAIN; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR STRUCTURE; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SUBUNITS; PURINE NUCLEOSIDES; PURINE-NUCLEOSIDE PHOSPHORYLASE; PYRIMIDINONES; THERMODYNAMICS; TRYPTOPHAN;

EID: 65449167640     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802339c     Document Type: Article

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