Ontology highlight
ABSTRACT:
SUBMITTER: Hopping G
PROVIDER: S-EPMC4091096 | biostudies-literature | 2014 Jul
REPOSITORIES: biostudies-literature
Hopping Gene G Kellock Jackson J Barnwal Ravi Pratap RP Law Peter P Bryers James J Varani Gabriele G Caughey Byron B Daggett Valerie V
eLife 20140715
Previous studies suggest that the toxic soluble-oligomeric form of different amyloid proteins share a common backbone conformation, but the amorphous nature of this oligomer prevents its structural characterization by experiment. Based on molecular dynamics simulations we proposed that toxic intermediates of different amyloid proteins adopt a common, nonstandard secondary structure, called α-sheet. Here we report the experimental characterization of peptides designed to be complementary to the α ...[more]