ArticleNature structural & molecular biology2025
Local structural flexibility drives oligomorphism in computationally designed protein assemblies.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Article
- Article
- Polymorphism in Self-Assembly of Short Peptoid Sequences.Polymer science & technology (Washington, D.C.) · 2026Article
- Bioinformatic and computational biophysics tools for nanopore engineering: a review from standard approaches to machine learning advancements.Journal of nanobiotechnology · 2026Review
- Mass spectrometry integrates protein design into structural biology method development.QRB discovery · 2026Review
- Natural Design of a Stabilized Cross-β Fold: Structure of the FuA FapC from Pseudomonas Sp. UK4 Reveals a Critical Role for Stacking of Imperfect Repeats.Advanced materials (Deerfield Beach, Fla.) · 2025Article
- Flexing protein assemblies.Nature structural & molecular biology · 2025Article
- Dynamic Assembly of Pentamer-Based Protein Nanotubes.ACS nano · 2025Article
- Atomically accurate de novo design of antibodies with RFdiffusion.bioRxiv : the preprint server for biology · 2025Article
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20 authors.
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Abstract
Many naturally occurring protein assemblies have dynamic structures that allow them to perform specialized functions. Although computational methods for designing novel self-assembling proteins have advanced substantially over the past decade, they primarily focus on designing static structures. Here we characterize three distinct computationally designed protein assemblies that exhibit unanticipated structural diversity arising from flexibility in their subunits. Cryo-EM single-particle reconstructions and native mass spectrometry reveal two distinct architectures for two assemblies, while six cryo-EM reconstructions for the third likely represent a subset of its solution-phase structures. Structural modeling and molecular dynamics simulations indicate that constrained flexibility within the subunits of each assembly promotes a defined range of architectures rather than nonspecific aggregation. Redesigning the flexible region in one building block rescues the intended monomorphic assembly. These findings highlight structural flexibility as a powerful design principle, enabling exploration of new structural and functional spaces in protein assembly design.
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