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FOR THE RECORD

Organism complexity anti-correlates with proteomic -aggregation propensity

Department of Biochemistry, University of Zürich, CH-8057 Zürich, Switzerland

(RECEIVED March 23, 2005; FINAL REVISION June 23, 2005; ACCEPTED June 24, 2005)

We introduce a novel approach to estimate differences in the -aggregation potential of eukaryotic proteomes. The approach is based on a statistical analysis of the -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 -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 -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.

Keywords: aggregation; protein aggregation propensity; proteome; intrinsically disordered proteins

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051473805.

Reprint requests to: Gian Gaetano Tartaglia or Amedeo Caflisch, Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland; e-mail: orgian{at}bioc.unizh.chorcaflisch@bioc.unizh.ch; fax: +41-44-635-68-62.

Supplemental material: see www.proteinscience.org

¹ These authors contributed equally to this work.

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