Micelle-like architecture of the monomer ensemble of Alzheimer's Amyloid-β peptide in aqueous solution and its implications for Aβ Aggregation

Journal of Molecular Biology

Volumn 403, Issue 1, 2010, Pages 148-165

  Vitalis, Andreas ^a   Caflisch, Amedeo ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

Author keywords

Alzheimer's disease; Conformational equilibria; Disorder; Hydrophobic interactions; Monte Carlo simulations

Indexed keywords

AMYLOID BETA PROTEIN; MONOMER; EMULSION; MICELLE;

ALZHEIMER DISEASE; AQUEOUS SOLUTION; ARTICLE; HYDROPHOBICITY; MICELLE; MONTE CARLO METHOD; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; TEMPERATURE; CHEMISTRY; COMPUTER SIMULATION; EMULSION; METABOLISM; NUCLEAR MAGNETIC RESONANCE; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

AMYLOID BETA-PEPTIDES; COMPUTER SIMULATION; EMULSIONS; MICELLES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN DENATURATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY;

EID: 77957256708     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.003     Document Type: Article

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