Influence of the hydrophobic interface and transition metal ions on the conformation of amyloidogenic model peptides

Biophysical Chemistry

Volumn 150, Issue 1-3, 2010, Pages 64-72

  Hoernke, M ^a   Koksch, B ^b   Brezesinski, G ^a  

^a MAX PLANCK INSTITUTE OF COLLOIDS AND INTERFACES   (Germany)

^b FREIE UNIVERSITÄT BERLIN   (Germany)

Author keywords

Amyloid formation; Hydrophobic interface; Metal ion complexation; Model peptide

Indexed keywords

AMYLOID; COPPER ION; METAL ION; ZINC ION; COPPER; ION; METAL; PEPTIDE; ZINC;

ALPHA HELIX; ARTICLE; BETA SHEET; BINDING SITE; CIRCULAR DICHROISM; COMPLEX FORMATION; CONTROLLED STUDY; HYDROPHOBICITY; INFRARED REFLECTION ABSORPTION SPECTROSCOPY; IONIC STRENGTH; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SPECTROSCOPY; X RAY DIFFRACTION; ALZHEIMER DISEASE; AMINO ACID SEQUENCE; CHEMICAL PHENOMENA; CHEMISTRY; HUMAN; METABOLISM; MOLECULAR GENETICS; PARKINSON DISEASE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID; BINDING SITES; CIRCULAR DICHROISM; COPPER; HUMANS; HYDROPHOBICITY; IONS; METALS; MOLECULAR SEQUENCE DATA; PARKINSON DISEASE; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; ZINC; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS;

EID: 77953702290     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2010.02.014     Document Type: Article

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