Aβ amyloid fibrils possess a core structure highly resistant to hydrogen exchange

Proceedings of the National Academy of Sciences of the United States of America

Volumn 97, Issue 25, 2000, Pages 13597-13601

  Kheterpal, Indu ^a   Zhou, Shaolian ^b,c   Cook, Kelsey D ^b   Wetzel, Ronald ^a  

^a UNIVERSITY OF TENNESSEE MEDICAL CENTER   (United States)

^b UNIVERSITY OF TENNESSEE   (United States)

^c Global Medical and Regulatory Writing   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID A PROTEIN; AMYLOID BETA PROTEIN; HYDROGEN; AMYLOID BETA PROTEIN[1-40]; PEPTIDE FRAGMENT;

ANALYTIC METHOD; ARTICLE; HYDROGEN BOND; MASS SPECTROMETRY; PH; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN SECONDARY STRUCTURE; SENILE PLAQUE; TEMPERATURE; AMINO ACID SEQUENCE; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; MOLECULAR GENETICS; PROTEIN CONFORMATION; REPRODUCIBILITY;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; HYDROGEN; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; REPRODUCIBILITY OF RESULTS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 0034610180     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.250288897     Document Type: Article

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