ArticleOpen biology2022
Modern and prebiotic amino acids support distinct structural profiles in proteins.
Article in Open biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Emergence and evolution of protein-coding de novo genes.Nature reviews. Genetics · 2026Review
- Prebiotic β-Strand Peptides May Be a Plausible Solution to the Protocell Permeability Problem.Journal of molecular evolution · 2026Review
- A highly limited amino acid library from asteroid Bennu yields wide-ranging protein folds.Nature communications · 2026Article
- Coenzyme-protein interactions since early life.eLife · 2025Article
- Prebiotically Plausible Peptides can Self-assemble into β-rich Nanostructures.bioRxiv : the preprint server for biology · 2025Article
- Folding and knotting of biotic and prebiotic amino acid sequences through reverse evolution.Biophysical journal · 2025Article
- Origins of Life: The Protein Folding Problem all over again?Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Peptides En Route from Prebiotic to Biotic Catalysis.Accounts of chemical research · 2024Article
- Xeno Amino Acids: A Look into Biochemistry as We Do Not Know It.Life (Basel, Switzerland) · 2023Review
- Experimental characterization of de novo proteins and their unevolved random-sequence counterparts.Nature ecology & evolution · 2023Article
- Early Selection of the Amino Acid Alphabet Was Adaptively Shaped by Biophysical Constraints of Foldability.Journal of the American Chemical Society · 2023Article
- Why we are made of proteins and nucleic acids: Structural biology views on extraterrestrial life.Biophysics and physicobiology · 2023Article
- Assessing structure and disorder prediction tools forF1000Research · 2023Article
- Modern and prebiotic amino acids support distinct structural profiles in proteins.Open biology · 2022Article
- Undefining life's biochemistry: implications for abiogenesis.Journal of the Royal Society, Interface · 2022Review
- Peptides before and during the nucleotide world: an origins story emphasizing cooperation between proteins and nucleic acids.Journal of the Royal Society, Interface · 2022Review
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The earliest proteins had to rely on amino acids available on early Earth before the biosynthetic pathways for more complex amino acids evolved. In extant proteins, a significant fraction of the 'late' amino acids (such as Arg, Lys, His, Cys, Trp and Tyr) belong to essential catalytic and structure-stabilizing residues. How (or if) early proteins could sustain an early biosphere has been a major puzzle. Here, we analysed two combinatorial protein libraries representing proxies of the available sequence space at two different evolutionary stages. The first is composed of the entire alphabet of 20 amino acids while the second one consists of only 10 residues (ASDGLIPTEV) representing a consensus view of plausibly available amino acids through prebiotic chemistry. We show that compact conformations resistant to proteolysis are surprisingly similarly abundant in both libraries. In addition, the early alphabet proteins are inherently more soluble and refoldable, independent of the general Hsp70 chaperone activity. By contrast, chaperones significantly increase the otherwise poor solubility of the modern alphabet proteins suggesting their coevolution with the amino acid repertoire. Our work indicates that while both early and modern amino acids are predisposed to supporting protein structure, they do so with different biophysical properties and via different mechanisms.
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