Estimating intrinsic structural preferences of de novo emerging random-sequence proteins: is aggregation the main bottleneck?
| Autor: | Annamária F. Ángyán, Zoltán Gáspári, András Perczel |
|---|---|
| Rok vydání: | 2012 |
| Předmět: |
Proteomics
Protein Conformation Biophysics De novo protein Biology Biochemistry Bottleneck Protein evolution Evolution Molecular chemistry.chemical_compound Mice Open Reading Frames Structural Biology Random sequence Structure prediction Genetics Animals Humans Nucleotide RNA Messenger Molecular Biology chemistry.chemical_classification Base Composition Genome Human Nucleotides Proteins Translation (biology) Cell Biology Sequence Analysis DNA Transmembrane protein chemistry Protein Biosynthesis DNA GC-content Aggregation propensity |
| Zdroj: | FEBS letters. 586(16) |
| ISSN: | 1873-3468 |
| Popis: | Present-day proteins are believed to have evolved features to reduce the risk of aggregation. However, proteins can emerge de novo by translation of non-coding DNA segments. In this study we assess the aggregation, disorder and transmembrane propensity of protein sequences generated by translating random nucleotide sequences of varying GC-content. Potential de novo random-sequence proteins translated from regions with GC content between 40% and 60% do not show stronger aggregation propensity than existing ones and exhibit similar tendency to be disordered. We suggest that de novo emerging proteins do not mean an unavoidable aggregation threat to evolving organisms. |
| Databáze: | OpenAIRE |
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