ArticleProtein science : a publication of the Protein Society2010
Comparative characterization of random-sequence proteins consisting of 5, 12, and 20 kinds of amino acids.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Prebiotically Plausible Peptides can Self-assemble into β-rich Nanostructures.bioRxiv : the preprint server for biology · 2025Article
- Xeno Amino Acids: A Look into Biochemistry as We Do Not Know It.Life (Basel, Switzerland) · 2023Review
- Early Selection of the Amino Acid Alphabet Was Adaptively Shaped by Biophysical Constraints of Foldability.Journal of the American Chemical Society · 2023Article
- Effect of the Addition of the Fifth Amino Acid to [GADV]-Protein on the Three-Dimensional Structure.Life (Basel, Switzerland) · 2023Article
- Modern and prebiotic amino acids support distinct structural profiles in proteins.Open biology · 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
- De novo proteins from random sequences through in vitro evolution.Current opinion in structural biology · 2021Review
- Enzyme catalysis prior to aromatic residues: Reverse engineering of a dephospho-CoA kinase.Protein science : a publication of the Protein Society · 2021Article
- Article
- Three dimensional structures of putative, primitive proteins to investigate the origin of homochirality.Scientific reports · 2019Article
- Pandoravirus Celtis Illustrates the Microevolution Processes at Work in the GiantFrontiers in microbiology · 2019Article
- Surveying the sequence diversity of model prebiotic peptides by mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Computational Redesign of Thioredoxin Is Hypersensitive toward Minor Conformational Changes in the Backbone Template.Journal of molecular biology · 2016Article
- Natural protein sequences are more intrinsically disordered than random sequences.Cellular and molecular life sciences : CMLS · 2016Article
- An RNA Binding Peptide Consisting of Four Types of Amino Acid by in Vitro Selection Using cDNA Display.ACS omega · 2016Article
- Evolution of new functions de novo and from preexisting genes.Cold Spring Harbor perspectives in biology · 2015Review
- Synthetic biology for the directed evolution of protein biocatalysts: navigating sequence space intelligently.Chemical Society reviews · 2015Review
- Proteins from an unevolved library of de novo designed sequences bind a range of small molecules.ACS synthetic biology · 2012Article
- Comparison of the frequency of functional SH3 domains with different limited sets of amino acids using mRNA display.PloS one · 2011Article
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4 authors.
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Abstract
Screening of functional proteins from a random-sequence library has been used to evolve novel proteins in the field of evolutionary protein engineering. However, random-sequence proteins consisting of the 20 natural amino acids tend to aggregate, and the occurrence rate of functional proteins in a random-sequence library is low. From the viewpoint of the origin of life, it has been proposed that primordial proteins consisted of a limited set of amino acids that could have been abundantly formed early during chemical evolution. We have previously found that members of a random-sequence protein library constructed with five primitive amino acids show high solubility (Doi et al., Protein Eng Des Sel 2005;18:279-284). Although such a library is expected to be appropriate for finding functional proteins, the functionality may be limited, because they have no positively charged amino acid. Here, we constructed three libraries of 120-amino acid, random-sequence proteins using alphabets of 5, 12, and 20 amino acids by preselection using mRNA display (to eliminate sequences containing stop codons and frameshifts) and characterized and compared the structural properties of random-sequence proteins arbitrarily chosen from these libraries. We found that random-sequence proteins constructed with the 12-member alphabet (including five primitive amino acids and positively charged amino acids) have higher solubility than those constructed with the 20-member alphabet, though other biophysical properties are very similar in the two libraries. Thus, a library of moderate complexity constructed from 12 amino acids may be a more appropriate resource for functional screening than one constructed from 20 amino acids.
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