The conformation of the prion domain of Sup35p in isolation and in the full-length protein

Angew Chem Int Ed Engl. 2013 Nov 25;52(48):12741-4. doi: 10.1002/anie.201304699. Epub 2013 Oct 9.
No abstract available

Keywords: Sup35p; fibrils; prions; proteins; solid-state NMR spectroscopy.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Nuclear Magnetic Resonance, Biomolecular
  • Peptide Termination Factors / chemistry*
  • Peptide Termination Factors / ultrastructure
  • Prions / chemistry*
  • Prions / ultrastructure
  • Protein Conformation
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae / ultrastructure
  • Saccharomyces cerevisiae Proteins / chemistry*
  • Saccharomyces cerevisiae Proteins / ultrastructure

Substances

  • Peptide Termination Factors
  • Prions
  • SUP35 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins