ArticleScience advances2016
Designing and defining dynamic protein cage nanoassemblies in solution.
Article in Science advances, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Construction of artificial organellesChemical science · 2025Review
- Information theory optimization of signals from small-angle scattering measurements.Biophysical journal · 2025Article
- Designed 2D protein crystals as dynamic molecular gatekeepers for a solid-state device.Nature communications · 2024Article
- X-ray crystal structure of a designed rigidified imaging scaffold in the ligand-free conformation.Acta crystallographica. Section F, Structural biology communications · 2024Article
- An interaction network approach predicts protein cage architectures in bionanotechnology.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Visualizing and accessing correlated SAXS data sets with Similarity Maps and Simple Scattering web resources.Methods in enzymology · 2023Article
- Protein Assembly by Design.Chemical reviews · 2021Review
- Designed folding pathway of modular coiled-coil-based proteins.Nature communications · 2021Article
- Diphenolic acid-modified PAMAM/chlorinated butyl rubber nanocomposites with superior mechanical, damping, and self-healing properties.Science and technology of advanced materials · 2021Article
- Allosteric cooperation in a de novo-designed two-domain protein.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Modular repeat protein sculpting using rigid helical junctions.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Engineering protein assemblies with allosteric control via monomer fold-switching.Nature communications · 2019Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- Review
- Article
- Robust Production, Crystallization, Structure Determination, and Analysis of [Fe-S] Proteins: Uncovering Control of Electron Shuttling and Gating in the Respiratory Metabolism of Molybdopterin Guanine Dinucleotide Enzymes.Methods in enzymology · 2018Article
- Targeting Allostery with Avatars to Design Inhibitors Assessed by Cell Activity: Dissecting MRE11 Endo- and Exonuclease Activities.Methods in enzymology · 2018Article
- Coiled coils unspring protein origami.Nature biotechnology · 2017Article
- Design of coiled-coil protein-origami cages that self-assemble in vitro and in vivo.Nature biotechnology · 2017Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Central challenges in the design of large and dynamic macromolecular assemblies for synthetic biology lie in developing effective methods for testing design strategies and their outcomes, including comprehensive assessments of solution behavior. We created and validated an advanced design of a 600-kDa protein homododecamer that self-assembles into a symmetric tetrahedral cage. The monomeric unit is composed of a trimerizing apex-forming domain genetically linked to an edge-forming dimerizing domain. Enhancing the crystallographic results, high-throughput small-angle x-ray scattering (SAXS) comprehensively contrasted our modifications under diverse solution conditions. To generate a phase diagram associating structure and assembly, we developed force plots that measure dissimilarity among multiple SAXS data sets. These new tools, which provided effective feedback on experimental constructs relative to design, have general applicability in analyzing the solution behavior of heterogeneous nanosystems and have been made available as a web-based application. Specifically, our results probed the influence of solution conditions and symmetry on stability and structural adaptability, identifying the dimeric interface as the weak point in the assembly. Force plots comparing SAXS data sets further reveal more complex and controllable behavior in solution than captured by our crystal structures. These methods for objectively and comprehensively comparing SAXS profiles for systems critically affected by solvent conditions and structural heterogeneity provide an enabling technology for advancing the design and bioengineering of nanoscale biological materials.
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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.