ArticleGenes2011
Protein folding absent selection.
Article in Genes, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Three Biopolymers and Origin of Life Scenarios.Life (Basel, Switzerland) · 2024Review
- Experimental characterization of de novo proteins and their unevolved random-sequence counterparts.Nature ecology & evolution · 2023Article
- Random peptides rich in small and disorder-promoting amino acids are less likely to be harmful.Genome biology and evolution · 2022Article
- 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
- CoLiDe: Combinatorial Library Design tool for probing protein sequence space.Bioinformatics (Oxford, England) · 2021Article
- Random protein sequences can form defined secondary structures and are well-tolerated in vivo.Scientific reports · 2017Article
- Foldability of a Natural De Novo Evolved Protein.Structure (London, England : 1993) · 2017Article
- Natural protein sequences are more intrinsically disordered than random sequences.Cellular and molecular life sciences : CMLS · 2016Article
- Chemical synthetic biology: a mini-review.Frontiers in microbiology · 2013Review
- The phylogenomic roots of modern biochemistry: origins of proteins, cofactors and protein biosynthesis.Journal of molecular evolution · 2012Article
- Evolution before genes.Biology direct · 2012Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological proteins are known to fold into specific 3D conformations. However, the fundamental question has remained: Do they fold because they are biological, and evolution has selected sequences which fold? Or is folding a common trait, widespread throughout sequence space? To address this question arbitrary, unevolved, random-sequence proteins were examined for structural features found in folded, biological proteins. Libraries of long (71 residue), random-sequence polypeptides, with ensemble amino acid composition near the mean for natural globular proteins, were expressed as cleavable fusions with ubiquitin. The structural properties of both the purified pools and individual isolates were then probed using circular dichroism, fluorescence emission, and fluorescence quenching techniques. Despite this necessarily sparse "sampling" of sequence space, structural properties that define globular biological proteins, namely collapsed conformations, secondary structure, and cooperative unfolding, were found to be prevalent among unevolved sequences. Thus, for polypeptides the size of small proteins, natural selection is not necessary to account for the compact and cooperative folded states observed in nature.
Identifiers
What OpenQuestion holds
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.