A self-assembled protein β-helix as a self-contained biofunctional motif.
Ontology highlight
ABSTRACT: Nature constructs matter by employing protein folding motifs, many of which have been synthetically reconstituted to exploit function. A less understood motif whose structure-function relationships remain unexploited is formed by parallel β-strands arranged in a helical repetitive pattern, termed a β-helix. Herein we reconstitute a protein β-helix by design and endow it with biological function. Unlike β-helical proteins, which are contiguous covalent structures, this β-helix self-assembles from an elementary sequence of 18 amino acids. Using a combination of experimental and computational methods, we demonstrate that the resulting assemblies are discrete cylindrical structures exhibiting conserved dimensions at the nanoscale. We provide evidence for the structures to form a carpet-like th
SUBMITTER: Dondi C
PROVIDER: S-EPMC12081914 | biostudies-literature | 2025 May
REPOSITORIES: biostudies-literature
ACCESS DATA