The conformation of the prion domain of Sup35 p in isolation and in the full-length protein

Angewandte Chemie - International Edition

Volumn 52, Issue 48, 2013, Pages 12741-12744

  Luckgei, Nina ^a   Schütz, Anne K ^b   Bousset, Luc ^c   Habenstein, Birgit ^a   Sourigues, Yannick ^c   Gardiennet, Carole ^a   Meier, Beat H ^b   Melki, Ronald ^c   Böckmann, Anja ^a  

^a UNIVERSITÉ LYON 1   (France)

^b ETH ZURICH   (Switzerland)

^c CNRS   (France)

Author keywords

fibrils; prions; proteins; solid state NMR spectroscopy; Sup35p

Indexed keywords

CONFORMATION ANALYSIS; FIBRILS; FULL-LENGTH PROTEINS; PRION PROTEIN; PRIONS; SOLID-STATE NMR SPECTROSCOPY; SUP35P;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

PROTEINS;

PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN; SUP35 PROTEIN, S CEREVISIAE; TRANSLATION TERMINATION FACTOR;

ARTICLE; CHEMISTRY; FIBRILS; NUCLEAR MAGNETIC RESONANCE; PRION; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SOLID-STATE NMR SPECTROSCOPY; SUP35P; ULTRASTRUCTURE;

FIBRILS; PRIONS; PROTEINS; SOLID-STATE NMR SPECTROSCOPY; SUP35P;

NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE TERMINATION FACTORS; PRIONS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 84887888765     PISSN: 14337851     EISSN: 15213773     Source Type: Journal    
DOI: 10.1002/anie.201304699     Document Type: Article

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