The yeast prion Ure2p retains its native α-helical conformation upon assembly into protein fibrils in vitro

EMBO Journal

Volumn 21, Issue 12, 2002, Pages 2903-2911

  Bousset, Luc ^a   Thomson, Neil H ^a   Radford, Sheena E ^a   Melki, Ronald ^a  

^a LABORATOIRE D ENZYMOLOGIE ET BIOCHIMIE STRUCTURALES   (France)

Author keywords

Amyloid fibrils; Atomic force microscopy; Conformational transition; Prion; Ure2p

Indexed keywords

AMYLOID; ASPARAGINE; GLUTAMINE; MONOMER; PRION PROTEIN; PROTEIN SUBUNIT; PROTEIN URE2P; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; ATOMIC FORCE MICROSCOPY; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; IN VITRO STUDY; MODEL; MOLECULAR INTERACTION; MUTAGENESIS; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN POLYMERIZATION; YEAST;

MICROSCOPY, ATOMIC FORCE; MODELS, MOLECULAR; PRIONS; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

EID: 0037124337     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/cdf303     Document Type: Article

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