Measurements of residual dipolar couplings in peptide inhibitors weakly aligned by transient binding to peptide amyloid fibrils

Journal of Biomolecular NMR

Volumn 29, Issue 4, 2004, Pages 525-530

  Chen, Zhongjing ^a,c   Reif, Bernd ^a,b  

^a LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

^b HUMBOLDT UNIVERSITY   (Germany)

^c TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Alzheimer's disease; Amyloid fibril; Beta sheet breaker peptide; Inhibitors of fibril formation; Protein aggregation; Solution state NMR spectroscopy; Transferred residual dipolar coupling; trRDC

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; CARBON; HYDROGEN; NITROGEN; PEPTIDE; PROTEIN INHIBITOR;

ARTICLE; BETA SHEET; CHEMICAL STRUCTURE; CONFORMATION; CONTROLLED STUDY; MAGNETIC FIELD; MEASUREMENT; MOLECULAR SIZE; POLARIZATION; PRIORITY JOURNAL; PROTEIN BINDING; SEQUENCE ALIGNMENT; STRUCTURE ANALYSIS;

AMYLOID; DATA INTERPRETATION, STATISTICAL; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES;

EID: 3242787273     PISSN: 09252738     EISSN: None     Source Type: Journal    
DOI: 10.1023/B:JNMR.0000034353.98902.4f     Document Type: Article

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