NMR-detected hydrogen exchange and molecular dynamics simulations provide structural insight into fibril formation of prion protein fragment 106-126

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

Volumn 100, Issue 25, 2003, Pages 14790-14795

  Kuwata, Kazuo ^a   Matumoto, Tomoharu ^b   Cheng, Hong ^c   Nagayama, Kuniaki ^b   James, Thomas L ^d   Roder, Heinrich ^c,e  

^a GIFU UNIVERSITY   (Japan)

^b NATIONAL INSTITUTE FOR PHYSIOLOGICAL SCIENCES   (Japan)

^c FOX CHASE CANCER CENTER   (United States)

^d UNIVERSITY OF CALIFORNIA   (United States)

^e UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; AMIDE; AMYLOID; HYDROGEN; MOUSE PRION PROTEIN[106-126]; PALINDROMIC DNA; PRION PROTEIN; PRION PROTEIN[106-126]; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; APOPTOSIS; ARTICLE; BETA SHEET; BOVINE SPONGIFORM ENCEPHALOPATHY; CELL DEATH; CELL PROLIFERATION; CIRCULAR DICHROISM; CREUTZFELDT JAKOB DISEASE; ELECTRON MICROSCOPY; FIBER; GLIA; HYPERTROPHY; MOLECULAR DYNAMICS; NERVE CELL; NEUROPATHOLOGY; PRION DISEASE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTON TRANSPORT;

ANIMALS; CIRCULAR DICHROISM; HYDROGEN; MAGNETIC RESONANCE SPECTROSCOPY; MICE; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; NEURONS; PEPTIDE FRAGMENTS; PEPTIDES; PRIONS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY;

BOVINAE;

EID: 0345598918     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.2433563100     Document Type: Article

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