The Alzheimer β-peptide shows temperature-dependent transitions between left-handed 31-helix, β-strand and random coil secondary structures

FEBS Journal

Volumn 272, Issue 15, 2005, Pages 3938-3949

  Danielsson, Jens ^a   Jarvet, Jüri ^a   Damberg, Peter ^a   Gräslund, Astrid ^a  

^a STOCKHOLM UNIVERSITY   (Sweden)

Author keywords

strand; Amyloid peptide; Left handed 31 helix; Random coil; Transition enthalpy

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40];

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; FIBER; HYDRODYNAMICS; HYDROPHILICITY; HYDROPHOBICITY; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; SENILE PLAQUE; TEMPERATURE DEPENDENCE;

ALZHEIMER DISEASE; AMYLOID BETA-PROTEIN; CIRCULAR DICHROISM; HUMANS; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, CHEMICAL; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE;

EID: 23644452100     PISSN: 1742464X     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2005.04812.x     Document Type: Article

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