Molecular dynamics simulations capture the misfolding of the bovine prion protein at acidic pH

Biomolecules

Volumn 4, Issue 1, 2014, Pages 181-201

  Cheng, Chin Jung ^a   Daggett, Valerie ^a  

^a University of Washington   (United States)

Author keywords

Amyloid disease; Mad cow disease; Molecular dynamics; Prion protein misfolding; PrPSc structure

Indexed keywords

PRION PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BOVINE SPONGIFORM ENCEPHALOPATHY; CHEMICAL PHENOMENA; MOLECULAR DOCKING; MOLECULAR DYNAMICS; NONHUMAN; PH; PROTEIN MISFOLDING; PROTEIN STRUCTURE; STRUCTURAL PROTEOMICS; ANIMAL; BOVINE; CHEMISTRY; METABOLISM; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE;

ANIMALS; CATTLE; ENCEPHALOPATHY, BOVINE SPONGIFORM; HYDROGEN-ION CONCENTRATION; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MOLECULAR DYNAMICS SIMULATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PRPC PROTEINS; PRPSC PROTEINS;

EID: 84928157591     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom4010181     Document Type: Article

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