Exchange, promiscuity, and orthogonality in de novo designed coiled-coil peptide assemblies

2024/12/09 by Kathleen W. Kurgan, Freddie J. O. Martin, William Dawson +3 · 1 voice
Materials Science · Biochemistry, Genetics and Molecular Biology · #Supramolecular Self-Assembly in Materials #Chemical Synthesis and Analysis #DNA and Nucleic Acid Chemistry

paper · pdf · doi:10.1039/d4sc06329e

openalex publication_date 2024/12/09 · openalex created_date 2025/10/10 · openalex updated_date 2026/07/22

Abstract

Dynamics and exchange between coiled-coil assemblies are evaluated by a fluorescence-based assay. De novo designed homo-dimers to heptamers are tested for faithful and promiscuous interactions, and re-designed to deliver an orthogonal set.

Citations

• De novoprotein design, a retrospective
• ColabFold: making protein folding accessible to all
• An atlas of protein homo-oligomerization across domains of life

Discussions

• NEW PUBLICATION: Exchange, promiscuity, and orthogonality in de novo designed coiled-coil peptide assemblies doi.org/10.1039/D4SC... [bsky, 1 points, 0 comments]

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