ArticleProceedings of the National Academy of Sciences of the United States of America2019
Consensus sequence design as a general strategy to create hyperstable, biologically active proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed.
- Initial efforts of translational development of AAV-encoded NaMolecular therapy. Advances · 2026Article
- Protein stability is determined by single-site bias rather than pairwise covariance.Nature chemical biology · 2026Article
- Development of advanced bioinformatic profiles to improve the detection and functional understanding of fungal acid phosphatases.Applied and environmental microbiology · 2026Article
- Rational Design of Hyoscyamine 6β-Hydroxylase for the Efficient Production of Scopolamine.Plant biotechnology journal · 2026Article
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- Engineering hyaluronic acid-binding cytokines for enhanced tumor retention and safety.bioRxiv : the preprint server for biology · 2026Article
- Tryptophanase Mining and Characterization toward the Biological Production of Indole Derivatives.ACS omega · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Engineering and Assay of Enzymes for Expanded Genetic Alphabet Replication.Biochemistry · 2025Article
- GArNet: A Genetic Algorithm-Based Protein Redesign Approach to Optimize Mutation Combinations Informed by Network Theory.Journal of chemical information and modeling · 2025Article
- Evolutionary-scale enzymology enables exploration of a rugged catalytic landscape.Science (New York, N.Y.) · 2025Article
- Characterization of a consensus-designedmBio · 2025Article
- Statistical Thermodynamics of the Protein Ensemble: Mediating Function and Evolution.Annual review of biophysics · 2025Review
- Engineered Oxalate Decarboxylase Boosts Activity and Stability for Biological Applications.ACS omega · 2025Article
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- Clone-specific residue changes at multiple positions are associated with amyloid formation by antibody light chains.Frontiers in immunology · 2025Article
- Design of ancestral mammalian alkaline phosphatase bearing high stability and productivity.Applied and environmental microbiology · 2024Article
- Ancestral Sequence Reconstruction to Enable Biocatalytic Synthesis of Azaphilones.Journal of the American Chemical Society · 2024Article
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- Article
18 more citing papers are in PubMed but not listed here.
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3 authors.
Funding
Abstract
Consensus sequence design offers a promising strategy for designing proteins of high stability while retaining biological activity since it draws upon an evolutionary history in which residues important for both stability and function are likely to be conserved. Although there have been several reports of successful consensus design of individual targets, it is unclear from these anecdotal studies how often this approach succeeds and how often it fails. Here, we attempt to assess generality by designing consensus sequences for a set of six protein families with a range of chain lengths, structures, and activities. We characterize the resulting consensus proteins for stability, structure, and biological activities in an unbiased way. We find that all six consensus proteins adopt cooperatively folded structures in solution. Strikingly, four of six of these consensus proteins show increased thermodynamic stability over naturally occurring homologs. Each consensus protein tested for function maintained at least partial biological activity. Although peptide binding affinity by a consensus-designed SH3 is rather low,
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