Slow spontaneous α-to-β structural conversion in a non-denaturing neutral condition reveals the intrinsically disordered property of the disulfide-reduced recombinant mouse prion protein

Prion

Volumn 6, Issue 5, 2012, Pages 489-497

  Sang, Jason C ^a,b   Lee, Chung Yu ^a   Luh, Frederick Y ^a   Huang, Ya Wen ^c   Chiang, Yun Wei ^c   Chen, Rita P Y ^a,b  

^a INSTITUTE OF BIOLOGICAL CHEMISTRY   (Taiwan)

^b NATIONAL TAIWAN UNIVERSITY   (Taiwan)

^c NATIONAL TSING HUA UNIVERSITY   (Taiwan)

Author keywords

Amyloid; Disulfide; EPR; ESR; Intrinsically disordered; Misfolding; Oligomer; Prion; Redox potential; SDSL

Indexed keywords

AMYLOID; BETA PRION PROTEIN OLIGOMER; CYSTEINE; MUTANT PROTEIN; OLIGOMER; PRION PROTEIN; RECOMBINANT PROTEIN; THIOFLAVINE; UNCLASSIFIED DRUG;

ALPHA HELIX; ANIMAL CELL; ARTICLE; BIOTRANSFORMATION; CIRCULAR DICHROISM; CONTROLLED STUDY; DISULFIDE BOND; FLUORESCENCE; MOUSE; NONHUMAN; PROTEIN DENATURATION; PROTEIN STRUCTURE; SPIN LABELING;

ANIMALS; BINDING SITES; BUFFERS; CIRCULAR DICHROISM; DISULFIDES; MICE; PEPTIDE FRAGMENTS; PRIONS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; THERMODYNAMICS;

EID: 84869823346     PISSN: 19336896     EISSN: 1933690X     Source Type: Journal    
DOI: 10.4161/pri.22217     Document Type: Article

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