English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

Significance Infectious proteins (prions) are capable of encoding genetic information by templating their conformation, just as DNA templates its sequence. The mechanism of this templating has not been clear. We provide definitive proof that the architecture of amyloid of the prion domain of yeast prion protein Sup35p is a folded in-register parallel β-sheet, and our data identify some of the sites of folds in the sheet. This architecture naturally suggests a templating mechanism based on favorable interactions among aligned side chains of identical amino acids. This is the only mechanism suggested to date for such a conformation templating.

Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid