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. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society.
Organism complexity anti-correlates with proteomic β-aggregation propensity / Tartaglia, G. G.; Pellarin, R.; Cavalli, A.; Caflisch, A.. - In: PROTEIN SCIENCE. - ISSN 0961-8368. - 14:10(2005), pp. 2735-2740. [10.1110/ps.051473805]
|Titolo:||Organism complexity anti-correlates with proteomic β-aggregation propensity|
|Data di pubblicazione:||2005|
|Citazione:||Organism complexity anti-correlates with proteomic β-aggregation propensity / Tartaglia, G. G.; Pellarin, R.; Cavalli, A.; Caflisch, A.. - In: PROTEIN SCIENCE. - ISSN 0961-8368. - 14:10(2005), pp. 2735-2740. [10.1110/ps.051473805]|
|Appartiene alla tipologia:||01a Articolo in rivista|