Mechanism of zinc(II)-promoted amyloid formation: Zinc(II) binding facilitates the transition from the partially α-helical conformer to aggregates of amyloid β protein(1-28)

Journal of Biological Inorganic Chemistry

Volumn 14, Issue 3, 2009, Pages 449-455

  Talmard, Christine ^a,b   Leuma Yona, Rodrigue ^a,b   Faller, Peter ^a  

^a CNRS   (France)

^b UNIVERSITÉ DE TOULOUSE   (France)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-28]; THIOFLAVINE; TRIFLUOROETHANOL; UNCLASSIFIED DRUG; ZINC ION;

ALPHA HELIX; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; FLUORESCENCE MICROSCOPY; METAL BINDING; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY; TURBIDIMETRY;

AMYLOID BETA-PROTEIN; BINDING SITES; PEPTIDE FRAGMENTS; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; TRIFLUOROETHANOL; ZINC;

EID: 61849148857     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00775-008-0461-9     Document Type: Article

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