Substantial contribution of the two imidazole rings of the His13-His14 dyad to Cu(II) binding in amyloid-β(1-16) at physiological pH and its significance

Journal of Physical Chemistry A

Volumn 115, Issue 34, 2011, Pages 9590-9602

  Shin, Byong Kyu ^a   Saxena, Sunil ^a  

^a UNIVERSITY OF PITTSBURGH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S DISEASE; AMINO ACID RESIDUES; BINDING MODES; COORDINATION ENVIRONMENT; CORRELATION SPECTROSCOPY; DOMINANT CONTRIBUTIONS; ELECTRON SPIN-ECHO ENVELOPE MODULATIONS; HIGH CONCENTRATION; HISTIDINE RESIDUES; HYPERFINES; MOLECULAR ORIGINS; PEPTIDE STRUCTURES; PH CHANGE; PHYSIOLOGICAL PH; SECONDARY STRUCTURES; SHEET STRUCTURE; SIDE-CHAINS; SPECTRAL SIMULATIONS;

AMINO ACIDS; BINDING ENERGY; ELECTRON SPIN RESONANCE SPECTROSCOPY; EXPERIMENTS; GLYCOPROTEINS; PEPTIDES; PHYSIOLOGY; SPIN DYNAMICS;

PH EFFECTS;

AMYLOID BETA PROTEIN; COPPER; HISTIDINE; IMIDAZOLE; IMIDAZOLE DERIVATIVE; PEPTIDE FRAGMENT;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; ARTICLE; BINDING SITE; CHEMISTRY; ELECTRON SPIN RESONANCE; HUMAN; METABOLISM; MOLECULAR GENETICS; PATHOPHYSIOLOGY; PH; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SPECTROSCOPY;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AMYLOID BETA-PEPTIDES; BINDING SITES; COPPER; ELECTRON SPIN RESONANCE SPECTROSCOPY; HISTIDINE; HUMANS; HYDROGEN-ION CONCENTRATION; IMIDAZOLES; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; SPECTRUM ANALYSIS;

EID: 80052210889     PISSN: 10895639     EISSN: 15205215     Source Type: Journal    
DOI: 10.1021/jp200379m     Document Type: Article

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