High affinity binding between copper and full-length prion protein identified by two different techniques

Journal of Biological Chemistry

Volumn 280, Issue 52, 2005, Pages 42750-42758

  Thompsett, Andrew R ^a   Abdelraheim, Salama R ^a   Daniels, Maki ^b   Brown, David R ^a,b  

^a University of Bath   (United Kingdom)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CALORIMETRY; COPPER; ISOTHERMS; PHYSIOLOGY; TITRATION;

COPPER BINDING; HISTIDINE; PRION PROTEINS;

PROTEINS;

COPPER; HISTIDINE; PRION PROTEIN; SUPEROXIDE DISMUTASE;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CONCENTRATION RESPONSE; CONTROLLED STUDY; ENZYME ACTIVITY; EXTRACELLULAR SPACE; ISOTHERM; MOUSE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; TECHNIQUE; TITRIMETRY; WILD TYPE;

ANIMALS; BINDING SITES; BIOCHEMISTRY; CALORIMETRY; CHELATING AGENTS; COPPER; ESCHERICHIA COLI; GLYCINE; HISTIDINE; HYDROGEN-ION CONCENTRATION; KINETICS; MICE; MUTAGENESIS; MUTATION; PRIONS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SUPEROXIDE DISMUTASE; TEMPERATURE;

EID: 30044443305     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M506521200     Document Type: Article

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