Molecular modelling indicates that the pathological conformations of prion proteins might be β-helical

Biochemical Journal

Volumn 343, Issue 2, 1999, Pages 453-460

  Downing, Donald T ^a   Lazo, N D ^a  

^a UNIVERSITY OF IOWA   (United States)

Author keywords

'Mad cow disease'; Bovine spongiform encephalopathy; Creutzfeldt Jakob disease; Scrapie

Indexed keywords

AMYLOID; CELL PROTEIN; ISOPROTEIN; PRION PROTEIN; PROTEIN PRECURSOR; SYNTHETIC PEPTIDE;

ARTICLE; BOVINE SPONGIFORM ENCEPHALOPATHY; CENTRAL NERVOUS SYSTEM INFECTION; CREUTZFELDT JAKOB DISEASE; HUMAN; KURU; MOLECULAR MODEL; NONHUMAN; PRION; PRION DISEASE; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; SCRAPIE;

AMINO ACID SEQUENCE; ANIMALS; CIRCULAR DICHROISM; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE FRAGMENTS; PRION DISEASES; PRIONS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN ISOFORMS; PROTEIN STRUCTURE, SECONDARY; REPETITIVE SEQUENCES, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

BOVINAE; MAMMALIA;

EID: 0033569687     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3430453     Document Type: Article

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