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Organism complexity anti-correlates with proteomic beta-aggregation propensity

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G.G. Tartaglia; R. Pellarin; A. Cavalli; A. Caflisch

Journal: Protein Sci.
Year: 2005
Volume: 14
Issue: 10
Pages: 2735-2740
DOI: 10.1110/ps.051473805
Type of Publication: Journal Article

Amino 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.