ArticleChemical science2017
Design and engineering of water-soluble light-harvesting protein maquettes.
Article in Chemical science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
17 citing papers in PubMed, 45 citations in OpenAlex.
- Unraveling Charge-Transfer States and Their Ultrafast Dynamics in Artificial Light-Harvesting Complexes.ACS physical chemistry Au · 2026Article
- Development of artificial photosystems based on designed proteins for mechanistic insights into photosynthesis.Protein science : a publication of the Protein Society · 2024Review
- De novo design of proteins housing excitonically coupled chlorophyll special pairs.Nature chemical biology · 2024Article
- Article
- Engineering excitonically coupled dimers in an artificial protein for light harvesting via computational modeling.Protein science : a publication of the Protein Society · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- De novo protein design of photochemical reaction centers.Nature communications · 2022Article
- Active control of strong plasmon-exciton coupling in biomimetic pigment-polymer antenna complexes grown by surface-initiated polymerisation from gold nanostructures.Chemical science · 2022Article
- Rational design of photosynthetic reaction center protein maquettes.Frontiers in molecular biosciences · 2022Article
- Designer Heme Proteins: Achieving Novel Function with Abiological Heme Analogues.Accounts of chemical research · 2021Article
- Recent Progress Using De Novo Design to Study Protein Structure, Design and Binding Interactions.Life (Basel, Switzerland) · 2021Review
- Review
- Designed for life: biocompatible de novo designed proteins and components.Journal of the Royal Society, Interface · 2018Review
- The ascent of man(made oxidoreductases).Current opinion in structural biology · 2018Review
- A synthetic biological quantum optical system.Nanoscale · 2018Article
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
Abstract
Natural selection in photosynthesis has engineered tetrapyrrole based, nanometer scale, light harvesting and energy capture in light-induced charge separation. By designing and creating nanometer scale artificial light harvesting and charge separating proteins, we have the opportunity to reengineer and overcome the limitations of natural selection to extend energy capture to new wavelengths and to tailor efficient systems that better meet human as opposed to cellular energetic needs. While tetrapyrrole cofactor incorporation in natural proteins is complex and often assisted by accessory proteins for cofactor transport and insertion, artificial protein functionalization relies on a practical understanding of the basic physical chemistry of protein and cofactors that drive nanometer scale self-assembly. Patterning and balancing of hydrophobic and hydrophilic tetrapyrrole substituents is critical to avoid natural or synthetic porphyrin and chlorin aggregation in aqueous media and speed cofactor partitioning into the non-polar core of a man-made water soluble protein designed according to elementary first principles of protein folding. This partitioning is followed by site-specific anchoring of tetrapyrroles to histidine ligands strategically placed for design control of rates and efficiencies of light energy and electron transfer while orienting at least one polar group towards the aqueous phase.
Identifiers
What OpenQuestion holds
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.