Transient formation of intermediate conformational states of amyloid-β peptide revealed by heteronuclear magnetic resonance spectroscopy

FEBS Letters

Volumn 585, Issue 7, 2011, Pages 1097-1102

  Yamaguchi, Takahiro ^a   Matsuzaki, Katsumi ^a   Hoshino, Masaru ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Amyloid fibril formation; Chemical exchange; Conformational change; NMR

Indexed keywords

AMYLOID BETA PROTEIN;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISSOCIATION; HETERONUCLEAR NUCLEAR MAGNETIC RESONANCE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE;

AMYLOID BETA-PEPTIDES; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, SECONDARY; TEMPERATURE; WATER;

EID: 79953250721     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.03.014     Document Type: Article

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