ArticleBiochimica et biophysica acta2016
First principles design of a core bioenergetic transmembrane electron-transfer protein.
Article in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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Who cites it
14 citing papers in PubMed.
- Computational design of de novo bioenergetic membrane proteins.Biochemical Society transactions · 2024Review
- Delineating redox cooperativity in water-soluble and membrane multiheme cytochromes through protein design.Protein science : a publication of the Protein Society · 2024Article
- Cellular production of a de novo membrane cytochrome.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- Review
- Designing minimalist membrane proteins.Biochemical Society transactions · 2019Review
- The de novo design of a biocompatible and functional integral membrane protein using minimal sequence complexity.Scientific reports · 2018Article
- The ascent of man(made oxidoreductases).Current opinion in structural biology · 2018Review
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- De novo synthetic biliprotein design, assembly and excitation energy transfer.Journal of the Royal Society, Interface · 2018Article
- Multi-step excitation energy transfer engineered in genetic fusions of natural and synthetic light-harvesting proteins.Journal of the Royal Society, Interface · 2017Article
- The soluble loop BC region guides, but not dictates, the assembly of the transmembrane cytochrome b6.PloS one · 2017Article
- Engineering an Artificial Flavoprotein Magnetosensor.Journal of the American Chemical Society · 2016Article
- De Novo Construction of Redox Active Proteins.Methods in enzymology · 2016Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Here we describe the design, Escherichia coli expression and characterization of a simplified, adaptable and functionally transparent single chain 4-α-helix transmembrane protein frame that binds multiple heme and light activatable porphyrins. Such man-made cofactor-binding oxidoreductases, designed from first principles with minimal reference to natural protein sequences, are known as maquettes. This design is an adaptable frame aiming to uncover core engineering principles governing bioenergetic transmembrane electron-transfer function and recapitulate protein archetypes proposed to represent the origins of photosynthesis. This article is part of a Special Issue entitled Biodesign for Bioenergetics--the design and engineering of electronic transfer cofactors, proteins and protein networks, edited by Ronald L. Koder and J.L. Ross Anderson.
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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.