ArticleChemical science2019
Engineering protein polymers of ultrahigh molecular weight
Article in Chemical science, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Merging Natural Biopolymers with Supramolecular Chemistry: Emulating the Native Extracellular Matrix's Complexity.ACS nano · 2025Review
- Genetically Engineered Liposwitch-Based Nanomaterials.Biomacromolecules · 2024Article
- Stimuli-Responsive Protein Hydrogels: Their Design, Properties, and Biomedical Applications.Polymers · 2023Review
- Non-Covalently Associated Streptavidin Multi-Arm Nanohubs Exhibit Mechanical and Thermal Stability in Cross-Linked Protein-Network Materials.Biomacromolecules · 2022Article
- Interdomain Linker Effect on the Mechanical Stability of Ig Domains in Titin.International journal of molecular sciences · 2022Article
- Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The giant muscle protein titin is the largest protein in cells and responsible for the passive elasticity of muscles. Titin, made of hundreds of individually folded globular domains, is a protein polymer with folded globular domains as its macromonomers. Due to titin's ultrahigh molecular weight, it has been challenging to engineer high molecular weight artificial protein polymers that mimic titin. Taking advantage of protein fragment reconstitution (PFR) of a small protein GB1, which can be reconstituted from its two split fragments G
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Registered trials
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