Ontology highlight
ABSTRACT:
SUBMITTER: Frederick KK
PROVIDER: S-EPMC4030713 | biostudies-literature | 2014 Feb
REPOSITORIES: biostudies-literature
Frederick Kendra K KK Debelouchina Galia T GT Kayatekin Can C Dorminy Tea T Jacavone Angela C AC Griffin Robert G RG Lindquist Susan S
Chemistry & biology 20140130 2
Yeast prions are self-templating protein-based mechanisms of inheritance whose conformational changes lead to the acquisition of diverse new phenotypes. The best studied of these is the prion domain (NM) of Sup35, which forms an amyloid that can adopt several distinct conformations (strains) that produce distinct phenotypes. Using magic-angle spinning nuclear magnetic resonance spectroscopy, we provide a detailed look at the dynamic properties of these forms over a broad range of timescales. We ...[more]