NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, Aβ(1-40)ox and Aβ(1-42)ox

European Journal of Biochemistry

Volumn 268, Issue 22, 2001, Pages 5930-5936

  Riek, Roland ^a   Güntert, Peter ^a   Döbeli, Heinz ^b   Wipf, Beat ^b   Wüthrich, Kurt ^a  

^a ETH ZURICH   (Switzerland)

^b F HOFFMANN LA ROCHE LTD   (Switzerland)

Author keywords

Aggregation; Alzheimer's disease; Aqueous solution; NMR; Polypeptide

Indexed keywords

AMINO ACID; AMYLOID BETA PROTEIN; METHIONINE SULFOXIDE;

ALZHEIMER DISEASE; AMINO ACID SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; COMPARATIVE STUDY; CONFORMATIONAL TRANSITION; GENETIC POLYMORPHISM; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN CONFORMATION; SENILE PLAQUE;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; CIRCULAR DICHROISM; HUMANS; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RECOMBINANT PROTEINS; SOLUTIONS; WATER;

EID: 0035173352     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0014-2956.2001.02537.x     Document Type: Article

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