Organism complexity anti-correlates with proteomic beta-aggregation propensity

TitleOrganism complexity anti-correlates with proteomic beta-aggregation propensity
Publication TypeJournal Article
Year of Publication2005
AuthorsTartaglia G.G, Pellarin R., Cavalli A., Caflisch A.
JournalProtein Science
Date Published2005 Oct
Type of ArticleResearch Article
KeywordsAmino Acid Sequence, Animals, Databases, Protein, Longevity, Models, Molecular, Protein Conformation, Protein Denaturation, Protein Folding, Proteins, Proteome

We introduce a novel approach to estimate differences in the β-aggregation potential of eukaryotic proteomes. The approach is based on a statistical analysis of the β-aggregation propensity of polypeptide segments, which is calculated by an equation derived from first principles using the physicochemical properties of the natural amino acids. Our analysis reveals a significant decreasing trend of the overall β-aggregation tendency with increasing organism complexity and longevity. A comparison with randomized proteomes shows that natural proteomes have a higher degree of polarization in both low and high β-aggregation prone sequences. The former originates from the requirement of intrinsically disordered proteins, whereas the latter originates from the necessity of proteins with a stable folded structure.



Alternate JournalProtein Sci.
PubMed ID16155201
PubMed Central IDPMC2253303
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