Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments

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

Volumn 100, Issue 26, 2003, Pages 15463-15468

  Fändrich, Marcus ^a   Forge, Vincent ^a,b   Buder, Katrin ^a   Kittler, Marlis ^a   Dobson, Christopher M ^a,c   Diekmann, Stephan ^a  

^a FRITZ LIPMANN INSTITUTE   (Germany)

^b CEA GRENOBLE   (France)

^c UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; APOMYOGLOBIN; MONOMER; MYOGLOBIN; POLYPEPTIDE;

ALPHA HELIX; ARTICLE; BETA SHEET; CIRCULAR DICHROISM; CORRELATION ANALYSIS; DENATURATION; FLUORESCENCE SPECTROSCOPY; INFRARED SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; TEMPERATURE SENSITIVITY; X RAY DIFFRACTION;

AMINO ACID SEQUENCE; ANIMALS; HORSES; MOLECULAR SEQUENCE DATA; MYOFIBRILS; MYOGLOBIN; PEPTIDES; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS; X-RAY DIFFRACTION;

EID: 0346734137     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0303758100     Document Type: Article

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