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
Volume14
Issue10
Pagination2735-2740
Date Published2005 Oct
Type of ArticleResearch Article
KeywordsAmino Acid Sequence, Animals, Databases, Protein, Longevity, Models, Molecular, Protein Conformation, Protein Denaturation, Protein Folding, Proteins, Proteome
Abstract

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.

DOI10.1110/ps.051473805
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Alternate JournalProtein Sci.
PubMed ID16155201
PubMed Central IDPMC2253303
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