Structure of the recombinant full-length hamster prion protein PrP(29-231): The N terminus is highly flexible

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

Volumn 94, Issue 25, 1997, Pages 13452-13457

  Donne, David G ^a   Viles, John H ^a   Groth, Darlene ^b   Mehlhorn, Ingrid ^b   James, Thomas L ^b,c   Cohen, Fred E ^b,c   Prusiner, Stanley B ^b   Wright, Peter E ^a   Dyson, H Jane ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Backbone dynamics; Conformational change; NMR structure

Indexed keywords

PRION PROTEIN; RECOMBINANT PROTEIN;

AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRION DISEASE; PRIORITY JOURNAL; PROTEIN SECONDARY STRUCTURE; SYRIAN HAMSTER;

AMINO ACID SEQUENCE; ANIMALS; CRICETINAE; ESCHERICHIA COLI; MAGNETIC RESONANCE SPECTROSCOPY; MESOCRICETUS; MICE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PRIONS; PROTEIN STRUCTURE, SECONDARY; PRPC PROTEINS; PRPSC PROTEINS; RECOMBINANT PROTEINS; SPECIES SPECIFICITY; THERMODYNAMICS;

CRICETINAE; MESOCRICETUS AURATUS;

EID: 0031456947     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.25.13452     Document Type: Article

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