ArticleNature communications2020
Assembly of a patchy protein into variable 2D lattices via tunable multiscale interactions.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
21 citing papers in PubMed.
- Impact of solvent forces and broken symmetry on the assembly of designed proteins at a liquid-solid interface.Nature communications · 2026Article
- Structural polymorphism of two-dimensional lattices assembled from baculoviral capsid proteins.Virologica Sinica · 2025Article
- Design of light- and chemically responsive protein assemblies through host-guest interactions.Chem · 2025Article
- Anisotropic DLVO-like interaction for charge patchiness in colloids and proteins.Nature communications · 2025Article
- Tuning the Dimensionality of Protein-Peptide Coassemblies to Build 2D Conductive Nanomaterials.ACS nano · 2025Article
- Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- A generic cross-seeding approach to protein crystallization.Journal of applied crystallography · 2025Article
- Interface flexibility controls the nucleation and growth of supramolecular networks.Nature chemistry · 2025Article
- Form Equals Function: Influence of Coacervate Architecture on Drug Delivery Applications.ACS biomaterials science & engineering · 2024Review
- Coupling of Spectrin Repeat Modules for the Assembly of Nanorods and Presentation of Protein Domains.ACS nano · 2024Article
- Two-dimensional silk.Science advances · 2024Article
- Designed 2D protein crystals as dynamic molecular gatekeepers for a solid-state device.Nature communications · 2024Article
- Self-assembly of nanocrystal checkerboard patterns via non-specific interactions.Nature communications · 2024Article
- Article
- Preparation and Unique Three-Dimensional Self-Assembly Property of Starfish Ferritin.Foods (Basel, Switzerland) · 2023Article
- Overcoming the entropy of polymer chains by making a plane with terminal groups: a thermoplastic PDMS with a long-range 1D structural order.Chemical science · 2023Article
- Self-sorting in macroscopic supramolecular self-assembly via additive effects of capillary and magnetic forces.Nature communications · 2022Article
- Arrow of Time, Entropy, and Protein Folding: Holistic View on Biochirality.International journal of molecular sciences · 2022Review
- Protein Assembly by Design.Chemical reviews · 2021Review
- Encoding hierarchical assembly pathways of proteins with DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Self-assembly of molecular building blocks into higher-order structures is exploited in living systems to create functional complexity and represents a powerful strategy for constructing new materials. As nanoscale building blocks, proteins offer unique advantages, including monodispersity and atomically tunable interactions. Yet, control of protein self-assembly has been limited compared to inorganic or polymeric nanoparticles, which lack such attributes. Here, we report modular self-assembly of an engineered protein into four physicochemically distinct, precisely patterned 2D crystals via control of four classes of interactions spanning Ångström to several-nanometer length scales. We relate the resulting structures to the underlying free-energy landscape by combining in-situ atomic force microscopy observations of assembly with thermodynamic analyses of protein-protein and -surface interactions. Our results demonstrate rich phase behavior obtainable from a single, highly patchy protein when interactions acting over multiple length scales are exploited and predict unusual bulk-scale properties for protein-based materials that ensue from such control.
Identifiers
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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.