Ontology highlight
ABSTRACT:
SUBMITTER: Nagarkar RP
PROVIDER: S-EPMC6032354 | biostudies-other | 2018 Jul
REPOSITORIES: biostudies-other
Protein science : a publication of the Protein Society 20180314 7
The repetitive self-assembled structure of amyloid can serve as inspiration to design functional materials. Herein, we describe the design of α/β6, a peptide that contains distinct α-helical and β-structure forming domains. The folding and association state of each domain can be controlled by temperature. At low temperatures, the α-domain favors a coiled-coil state while the β-domain is unstructured. Irreversible fibril formation via self-assembly of the β-domain is triggered at high temperature ...[more]