Preferential Cu2+ coordination by His96 and His 111 induces β-sheet formation in the unstructured amyloiodogenic region of the prion protein

Journal of Biological Chemistry

Volumn 279, Issue 31, 2004, Pages 32018-32027

  Jones, Christopher E ^b   Abdelraheim, Salama R ^a   Brown, David E ^a   Viles, John H ^b  

^a University of Bath   (United Kingdom)

^b QUEEN MARY UNIVERSITY OF LONDON   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CELL CULTURE; COPPER; ELECTROMAGNETIC WAVES; GLUCOSE; NUCLEAR MAGNETIC RESONANCE;

BINDING CELLS; COPPER BINDING;

PROTEINS;

AMINO ACID; COPPER; GLYCOPROTEIN; HISTIDINE; PRION PROTEIN; AMYLOID; GLYCINE; LIGAND; PEPTIDE;

ARTICLE; CIRCULAR DICHROISM; ELECTRON SPIN RESONANCE; METAL BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; SPECTROSCOPY; ANIMAL; BINDING SITE; CHEMISTRY; MOUSE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE SYNTHESIS; PH; PRION; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; SPECTROPHOTOMETRY; ULTRAVIOLET RADIATION;

AMYLOID; ANIMALS; BINDING SITES; CIRCULAR DICHROISM; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; GLYCINE; HISTIDINE; HYDROGEN-ION CONCENTRATION; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MICE; PEPTIDE BIOSYNTHESIS; PEPTIDES; PRIONS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROPHOTOMETRY; ULTRAVIOLET RAYS;

EID: 3542999252     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M403467200     Document Type: Article

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