ArticleNature communications2021
Structural resolution of switchable states of a de novo peptide assembly.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Self-assembling protein cages: from coiled-coil module to machine learning-drivenMaterials advances · 2026Review
- Sequence Prediction, Structural Modelling and the Challenges of Plasticity in Coiled Coils.Sub-cellular biochemistry · 2026Review
- Protein A-like peptide generation based on generalized diffusion model.Journal of computer-aided molecular design · 2025Article
- Assessment of the Topology and Oligomerisation States of Coiled Coils Using Metadynamics with Conformational Restraints.Journal of chemical theory and computation · 2025Article
- Exploration of the hierarchical assembly space of collagen-like peptides beyond the triple helix.Nature communications · 2024Article
- Rationally seeded computational protein design of ɑ-helical barrels.Nature chemical biology · 2024Article
- A de novo designed coiled coil-based switch regulates the microtubule motor kinesin-1.Nature chemical biology · 2024Article
- Beyond the Triple Helix: Exploration of the Hierarchical Assembly Space of Collagen-like Peptides.bioRxiv : the preprint server for biology · 2024Article
- Metal-Promoted Higher-Order Assembly of Disulfide-Stapled Helical Barrels.Nanomaterials (Basel, Switzerland) · 2023Article
- Rational Design of Phosphorylation-Responsive Coiled Coil-Peptide Assemblies.ACS synthetic biology · 2023Article
- Protein design via deep learning.Briefings in bioinformatics · 2022Review
- Rational design of hairpin RNA excited states reveals multi-step transitions.Nature communications · 2022Article
- Computational Design of Single-Peptide Nanocages with Nanoparticle Templating.Molecules (Basel, Switzerland) · 2022Article
- Design principles of protein switches.Current opinion in structural biology · 2022Review
- Coiled coils 9-to-5: rationalChemical science · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
De novo protein design is advancing rapidly. However, most designs are for single states. Here we report a de novo designed peptide that forms multiple α-helical-bundle states that are accessible and interconvertible under the same conditions. Usually in such designs amphipathic α helices associate to form compact structures with consolidated hydrophobic cores. However, recent rational and computational designs have delivered open α-helical barrels with functionalisable cavities. By placing glycine judiciously in the helical interfaces of an α-helical barrel, we obtain both open and compact states in a single protein crystal. Molecular dynamics simulations indicate a free-energy landscape with multiple and interconverting states. Together, these findings suggest a frustrated system in which steric interactions that maintain the open barrel and the hydrophobic effect that drives complete collapse are traded-off. Indeed, addition of a hydrophobic co-solvent that can bind within the barrel affects the switch between the states both in silico and experimentally.
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