Organism complexity anti-correlates with proteomic beta-aggregation propensity
| Title | Organism complexity anti-correlates with proteomic beta-aggregation propensity |
| Publication Type | Journal Article |
| Year of Publication | 2005 |
| Authors | Tartaglia G.G, Pellarin R., Cavalli A., Caflisch A. |
| Journal | Protein Science |
| Volume | 14 |
| Issue | 10 |
| Pagination | 2735-2740 |
| Date Published | 2005 Oct |
| Type of Article | Research Article |
| ISSN | 0961-8368 |
| Keywords | Amino Acid Sequence, Animals, Databases, Protein, Longevity, Models, Molecular, Protein Conformation, Protein Denaturation, Protein Folding, Proteins, Proteome |
| Abstract | 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. |
| DOI | 10.1110/ps.051473805 |
| pubindex | 0070 |
| Alternate Journal | Protein Sci. |
| PubMed ID | 16155201 |
| PubMed Central ID | PMC2253303 |
