ArticleCellular and molecular life sciences : CMLS2016
Natural protein sequences are more intrinsically disordered than random sequences.
Article in Cellular and molecular life sciences : CMLS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Oncogenic roles of young human de novo genes and their potential as neoantigens in cancer immunotherapy.Cell genomics · 2025Article
- Exo-Tox: Identifying Exotoxins from secreted bacterial proteins.BioData mining · 2025Article
- Active learning of the thermodynamics-dynamics trade-off in protein condensates.Science advances · 2024Article
- Sequence-based Functional Metagenomics Reveals Novel Natural Diversity of Functional CopA in Environmental Microbiomes.Genomics, proteomics & bioinformatics · 2023Article
- Experimental characterization of de novo proteins and their unevolved random-sequence counterparts.Nature ecology & evolution · 2023Article
- Modern and prebiotic amino acids support distinct structural profiles in proteins.Open biology · 2022Article
- Characterization of intrinsically disordered regions in proteins informed by human genetic diversity.PLoS computational biology · 2022Article
- The Effects of Sequence Length and Composition of Random Sequence Peptides on the Growth ofGenes · 2021Article
- Exploring Potential Signals of Selection for Disordered Residues in Prokaryotic and Eukaryotic Proteins.Genomics, proteomics & bioinformatics · 2020Article
- SPOT-Disorder2: Improved Protein Intrinsic Disorder Prediction by Ensembled Deep Learning.Genomics, proteomics & bioinformatics · 2019Article
- The Evolutionary Consequences of Transposon-Related Pericentromer Expansion in Melon.Genome biology and evolution · 2018Article
- Random protein sequences can form defined secondary structures and are well-tolerated in vivo.Scientific reports · 2017Article
- Mass & secondary structure propensity of amino acids explain their mutability and evolutionary replacements.Scientific reports · 2017Article
- Young Genes are Highly Disordered as Predicted by the Preadaptation Hypothesis ofNature ecology & evolution · 2017Article
- Order, Disorder, and Everything in Between.Molecules (Basel, Switzerland) · 2016Review
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Authors and funding
8 authors.
Funding
Abstract
Most natural protein sequences have resulted from millions or even billions of years of evolution. How they differ from random sequences is not fully understood. Previous computational and experimental studies of random proteins generated from noncoding regions yielded inclusive results due to species-dependent codon biases and GC contents. Here, we approach this problem by investigating 10,000 sequences randomized at the amino acid level. Using well-established predictors for protein intrinsic disorder, we found that natural sequences have more long disordered regions than random sequences, even when random and natural sequences have the same overall composition of amino acid residues. We also showed that random sequences are as structured as natural sequences according to contents and length distributions of predicted secondary structure, although the structures from random sequences may be in a molten globular-like state, according to molecular dynamics simulations. The bias of natural sequences toward more intrinsic disorder suggests that natural sequences are created and evolved to avoid protein aggregation and increase functional diversity.
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