ArticlePloS one2011
De novo designed proteins from a library of artificial sequences function in Escherichia coli and enable cell growth.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 109 citations in OpenAlex.
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- Crystal structure and activity of a de novo enzyme, ferric enterobactin esterase Syn-F4.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Rescue ofeLife · 2023Article
- A de novo protein catalyzes the synthesis of semiconductor quantum dots.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Tailorable Tetrahelical Bundles as a Toolkit for Redox Studies.The journal of physical chemistry. B · 2022Article
- Peptides before and during the nucleotide world: an origins story emphasizing cooperation between proteins and nucleic acids.Journal of the Royal Society, Interface · 2022Review
- Protein-protein interaction prediction with deep learning: A comprehensive review.Computational and structural biotechnology journal · 2022Review
- De novo proteins from random sequences through in vitro evolution.Current opinion in structural biology · 2021Review
- CoLiDe: Combinatorial Library Design tool for probing protein sequence space.Bioinformatics (Oxford, England) · 2021Article
- Substitution of a Surface-Exposed Residue Involved in an Allosteric Network Enhances Tryptophan Synthase Function in Cells.Frontiers in molecular biosciences · 2021Article
- Deep Learning in Protein Structural Modeling and Design.Patterns (New York, N.Y.) · 2020Review
- The temperature dependence of amino acid hydrophobicity data is related to the genetic coding algorithm for complementary (sense and antisense) peptide interactions.Data in brief · 2020Article
- A Strategy for Combinatorial Cavity Design in De Novo Proteins.Life (Basel, Switzerland) · 2020Article
- MinimalistACS catalysis · 2019Article
- Thawing out frozen metabolic accidents.BMC biology · 2019Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A central challenge of synthetic biology is to enable the growth of living systems using parts that are not derived from nature, but designed and synthesized in the laboratory. As an initial step toward achieving this goal, we probed the ability of a collection of >10(6) de novo designed proteins to provide biological functions necessary to sustain cell growth. Our collection of proteins was drawn from a combinatorial library of 102-residue sequences, designed by binary patterning of polar and nonpolar residues to fold into stable 4-helix bundles. We probed the capacity of proteins from this library to function in vivo by testing their abilities to rescue 27 different knockout strains of Escherichia coli, each deleted for a conditionally essential gene. Four different strains--ΔserB, ΔgltA, ΔilvA, and Δfes--were rescued by specific sequences from our library. Further experiments demonstrated that a strain simultaneously deleted for all four genes was rescued by co-expression of four novel sequences. Thus, cells deleted for ∼0.1% of the E. coli genome (and ∼1% of the genes required for growth under nutrient-poor conditions) can be sustained by sequences designed de novo.
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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.