Organism complexity anti-correlates with proteomic beta-aggregation propensity

Protein Sci. 2005 Oct;14(10):2735-40. doi: 10.1110/ps.051473805. Epub 2005 Sep 9.


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

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Databases, Protein
  • Longevity
  • Models, Molecular*
  • Protein Conformation
  • Protein Denaturation
  • Protein Folding*
  • Proteins / chemistry*
  • Proteome*


  • Proteins
  • Proteome