ArticleScience (New York, N.Y.)2022
Reconfigurable asymmetric protein assemblies through implicit negative design.
Article in Science (New York, N.Y.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed.
- Computational design of metalloproteases.Nature · 2026Article
- A Generative Neuro-Symbolic AI for Protein Sequence Design.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Article
- Clocked stepping of an artificial protein walker along a DNA track.Nature nanotechnology · 2026Article
- Microscale Mechanical Cues in Hydrogels: Engineering Strategies to Modulate Cell Fates in Three Dimensions.Cell biomaterials · 2026Article
- Negative design enables cell-free expression and folding of designed transmembrane β-barrels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Review
- Using experimental results of protein design to guide biomolecular energy-function development.PLoS computational biology · 2026Article
- Thermally Induced Reassembly of Ginger Extracellular Vesicles for Oral Therapy of Intestinal Inflammation.Research (Washington, D.C.) · 2026Article
- De novo design of light-responsive protein-protein interactions enables reversible formation of protein assemblies.Nature chemistry · 2025Article
- Computational design of metalloproteases.bioRxiv : the preprint server for biology · 2025Article
- Article
- Bond-centric modular design of protein assemblies.Nature materials · 2025Article
- Article
- Article
- Design of high-affinity binders to immune modulating receptors for cancer immunotherapy.Nature communications · 2025Article
- Article
- Article
- Prediction of the Stability of Protein Substructures Using AI/ML Techniques.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Design of pseudosymmetric protein hetero-oligomers.Nature communications · 2024Article
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Asymmetric multiprotein complexes that undergo subunit exchange play central roles in biology but present a challenge for design because the components must not only contain interfaces that enable reversible association but also be stable and well behaved in isolation. We use implicit negative design to generate β sheet-mediated heterodimers that can be assembled into a wide variety of complexes. The designs are stable, folded, and soluble in isolation and rapidly assemble upon mixing, and crystal structures are close to the computational models. We construct linearly arranged hetero-oligomers with up to six different components, branched hetero-oligomers, closed C4-symmetric two-component rings, and hetero-oligomers assembled on a cyclic homo-oligomeric central hub and demonstrate that such complexes can readily reconfigure through subunit exchange. Our approach provides a general route to designing asymmetric reconfigurable protein systems.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.