Organism complexity anti-correlates with proteomic beta-aggregation propensity.
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.
Tartaglia
Gian Gaetano
GG
Department of Biochemistry, University of Zürich, Winterthurerstrasse 190, CH-8057 Zürich, Switzerland. gian@bioc.unizh.ch
Pellarin
Riccardo
R
Cavalli
Andrea
A
Caflisch
Amedeo
A
D000595:Amino Acid Sequence; D000818:Animals; D030562:Databases, Protein; D008136:Longevity; D008958:Models, Molecular; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D020543:Proteome
D011506:Proteins; D020543:Proteome