ArticleNature communications2021
Designed folding pathway of modular coiled-coil-based proteins.
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 12 papers.
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Who cites it
12 citing papers in PubMed, 22 citations in OpenAlex.
- 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
- Programmable Protein-DNA Composite Nanostructures: from Nanostructure Construction to Protein-Induced Micro-Scale Material Self-Assembly and Functionalization.Small (Weinheim an der Bergstrasse, Germany) · 2025Article
- Beyond Dimerization: Harnessing Tetrameric Coiled-Coils for Nanostructure Assembly.Angewandte Chemie (International ed. in English) · 2025Article
- Preorganized cyclic modules facilitate the self-assembly of protein nanostructures.Chemical science · 2024Article
- Computational Prediction of Coiled-Coil Protein Gelation Dynamics and Structure.Biomacromolecules · 2024Article
- Crystal Structure ofJournal of the American Chemical Society · 2023Article
- A multiplexed bacterial two-hybrid for rapid characterization of protein-protein interactions and iterative protein design.Nature communications · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Strategies for Controlling the Spatial Orientation of Single Molecules Tethered on DNA Origami Templates Physisorbed on Glass Substrates: Intercalation and Stretching.International journal of molecular sciences · 2022Article
- A nanobody toolbox targeting dimeric coiled-coil modules for functionalization of designed protein origami structures.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Novel Regeneration Approach for Creating Reusable FO-SPR Probes with NTA Surface Chemistry.Nanomaterials (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Natural proteins are characterised by a complex folding pathway defined uniquely for each fold. Designed coiled-coil protein origami (CCPO) cages are distinct from natural compact proteins, since their fold is prescribed by discrete long-range interactions between orthogonal pairwise-interacting coiled-coil (CC) modules within a single polypeptide chain. Here, we demonstrate that CCPO proteins fold in a stepwise sequential pathway. Molecular dynamics simulations and stopped-flow Förster resonance energy transfer (FRET) measurements reveal that CCPO folding is dominated by the effective intra-chain distance between CC modules in the primary sequence and subsequent folding intermediates, allowing identical CC modules to be employed for multiple cage edges and thus relaxing CCPO cage design requirements. The number of orthogonal modules required for constructing a CCPO tetrahedron can be reduced from six to as little as three different CC modules. The stepwise modular nature of the folding pathway offers insights into the folding of tandem repeat proteins and can be exploited for the design of modular protein structures based on a given set of orthogonal modules.
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