@article{bibcite_162,
  keywords = {Models, Molecular, Protein Denaturation, Protein Folding, Animals, Protein Conformation, Amino Acid Sequence, Proteins, Databases, Protein, Longevity, Proteome},
  author = {G. G. Tartaglia and R. Pellarin and A. Cavalli and A. Caflisch},
  title = {Organism complexity anti-correlates with proteomic beta-aggregation propensity},
  abstract = {<p>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.</p>},
  year = {2005},
  journal = {Protein Science},
  volume = {14},
  pages = {2735-2740},
  month = {2005 Oct},
  issn = {0961-8368},
  doi = {10.1110/ps.051473805},
  language = {eng},
}