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Estimating intrinsic structural preferences of de novo emerging random‐sequence proteins: Is aggregation the main bottleneck?
Author(s) -
Ángyán Annamária F.,
Perczel András,
Gáspári Zoltán
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.06.007
Subject(s) - sequence (biology) , computational biology , biology , transmembrane protein , random sequence , genetics , mathematics , mathematical analysis , receptor , distribution (mathematics)
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.