ArticleProceedings of the National Academy of Sciences of the United States of America2013
Simplified protein design biased for prebiotic amino acids yields a foldable, halophilic protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 111 citations in OpenAlex.
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- A highly limited amino acid library from asteroid Bennu yields wide-ranging protein folds.Nature communications · 2026Article
- Molecular Complexity Constrained Early Amino Acid Recruitment into the Genetic Code.Genome biology and evolution · 2026Article
- RNA binding and coacervation promote preservation of peptide form and function across the heterochiral-homochiral divide.Protein science : a publication of the Protein Society · 2025Article
- How sensitive are protein hydration shells to electrolyte concentration and protein composition?Protein science : a publication of the Protein Society · 2025Article
- Comparative analysis of reconstructed ancestral proteins with their extant counterparts suggests primitive life had an alkaline habitat.Scientific reports · 2024Article
- Xeno Amino Acids: A Look into Biochemistry as We Do Not Know It.Life (Basel, Switzerland) · 2023Review
- Prevalence and mechanism of synergistic carboxylate-cation-water interactions in halophilic proteins.Biophysical journal · 2023Article
- Why we are made of proteins and nucleic acids: Structural biology views on extraterrestrial life.Biophysics and physicobiology · 2023Article
- A Short Tale of the Origin of Proteins and Ribosome Evolution.Microorganisms · 2022Review
- Peptide-RNA Coacervates as a Cradle for the Evolution of Folded Domains.Journal of the American Chemical Society · 2022Article
- A Closer Look at Non-random Patterns Within Chemistry Space for a Smaller, Earlier Amino Acid Alphabet.Journal of molecular evolution · 2022Article
- Modern and prebiotic amino acids support distinct structural profiles in proteins.Open biology · 2022Article
- Probing the Role of Cysteine Thiyl Radicals in Biology: Eminently Dangerous, Difficult to Scavenge.Antioxidants (Basel, Switzerland) · 2022Review
- In Vitro Evolution Reveals Noncationic Protein-RNA Interaction Mediated by Metal Ions.Molecular biology and evolution · 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
- Amino Acid Specificity of Ancestral Aminoacyl-tRNA Synthetase Prior to the Last Universal Common Ancestor Commonote commonote.Journal of molecular evolution · 2022Article
- The Mutational Robustness of the Genetic Code and Codon Usage in Environmental Context: A Non-Extremophilic Preference?Life (Basel, Switzerland) · 2021Article
- Enzyme catalysis prior to aromatic residues: Reverse engineering of a dephospho-CoA kinase.Protein science : a publication of the Protein Society · 2021Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A compendium of different types of abiotic chemical syntheses identifies a consensus set of 10 "prebiotic" α-amino acids. Before the emergence of biosynthetic pathways, this set is the most plausible resource for protein formation (i.e., proteogenesis) within the overall process of abiogenesis. An essential unsolved question regarding this prebiotic set is whether it defines a "foldable set"--that is, does it contain sufficient chemical information to permit cooperatively folding polypeptides? If so, what (if any) characteristic properties might such polypeptides exhibit? To investigate these questions, two "primitive" versions of an extant protein fold (the β-trefoil) were produced by top-down symmetric deconstruction, resulting in a reduced alphabet size of 12 or 13 amino acids and a percentage of prebiotic amino acids approaching 80%. These proteins show a substantial acidification of pI and require high salt concentrations for cooperative folding. The results suggest that the prebiotic amino acids do comprise a foldable set within the halophile environment.
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