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Volumn 48, Issue 49, 2009, Pages 9273-9276
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Pulse EPR spectroscopy reveals the coordination sphere of copper(II) Ions in the 1-16 amyloid-β peptide: A key role of the first two N-terminus residues
c
CEA GRENOBLE
(France)
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Author keywords
Amyloid peptides; Bioinorganic chemistry; Copper; Epr spectroscopy; Ligand interactions
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Indexed keywords
ALZHEIMER'S DISEASE;
BIOINORGANIC CHEMISTRY;
COORDINATION SPHERE;
COPPER IONS;
CU IONS;
EPR SPECTROSCOPY;
ISOTOPIC LABELING;
LIGAND INTERACTIONS;
PHYSIOLOGICAL PH;
PULSE EPR;
AMINES;
AMINO ACIDS;
BIOCHEMISTRY;
COPPER;
ELECTRON RESONANCE;
GLYCOPROTEINS;
LIGANDS;
ORGANIC ACIDS;
PARAMAGNETIC RESONANCE;
PEPTIDES;
PH EFFECTS;
QUANTUM THEORY;
ELECTRON SPIN RESONANCE SPECTROSCOPY;
AMYLOID BETA PROTEIN;
COPPER;
ION;
REACTIVE OXYGEN METABOLITE;
ALZHEIMER DISEASE;
ANIMAL;
ARTICLE;
CHEMICAL STRUCTURE;
CHEMISTRY;
ELECTRON SPIN RESONANCE;
HUMAN;
METABOLISM;
METHODOLOGY;
PATHOLOGY;
ALZHEIMER DISEASE;
AMYLOID BETA-PROTEIN;
ANIMALS;
COPPER;
ELECTRON SPIN RESONANCE SPECTROSCOPY;
HUMANS;
IONS;
MOLECULAR STRUCTURE;
REACTIVE OXYGEN SPECIES;
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EID: 72949092936
PISSN: 14337851
EISSN: None
Source Type: Journal
DOI: 10.1002/anie.200904567 Document Type: Article |
Times cited : (170)
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References (22)
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