The octapeptide repeats in mammalian prion protein constitute a pH-dependent folding and aggregation site

Journal of Molecular Biology

Volumn 334, Issue 3, 2003, Pages 477-488

  Zahn, Ralph ^a,b  

^a ETH ZURICH   (Switzerland)

^b ALICON GmbH   (Switzerland)

Author keywords

NMR structure; Octapeptide repeats; pH dependent conformation; Prion protein; Protein aggregation

Indexed keywords

COPPER ION; GLUTAMINYLPROLYLHISTIDYLGLYCYLGLYCYLGLYCYLTRYPTOPHYLGLYCINE; GLYCYLGLUTAMINYLPROLYLHISTIDYLGLYCYLGLYCYLGLYCYLTRYPTOPHAN; GLYCYLGLYCYLGLYCYLTRYPTOPHYLGLYCYLGLUTAMINYLPROLYLHISTIDINE; GLYCYLGLYCYLTRYPTOPHYLGLYCYLGLUTAMINYLPROLYLHISTIDYLGLYCINE; GLYCYLTRYPTOPHYLGLYCYLGLUTAMINYLPROLYLHISTIDYLGLYCYLGLYCINE; HISTIDYLGLYCYLGLYCYLGLYCYLTRYPTOPHYLGLYCYLGLUTAMINYLPROLINE; OCTAPEPTIDE; PEPTIDE FRAGMENT; PRION PROTEIN; PROLYLHISTIDYLGLYCYLGLYCYLGLYCYLTRYPTOPHYLGLYCYLGLUTAMINE; RECOMBINANT PROTEIN; TRYPTOPHYLGLYCYLGLUTAMINYLPROLYLHISTIDYLGLYCYLGLYCYLGLYCINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CELL MEMBRANE; CELL PH; CONFORMATIONAL TRANSITION; CRYSTAL STRUCTURE; METAL BINDING; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; NUCLEOTIDE SEQUENCE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REGULATORY MECHANISM; STRUCTURE ANALYSIS;

MAMMALIA;

EID: 0242662244     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.048     Document Type: Article

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