<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Tartaglia, GG.</style></author><author><style face="normal" font="default" size="100%">Pellarin, R.</style></author><author><style face="normal" font="default" size="100%">Cavalli, A.</style></author><author><style face="normal" font="default" size="100%">Caflisch, A.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Organism complexity anti-correlates with proteomic beta-aggregation propensity.</style></title><secondary-title><style face="normal" font="default" size="100%">Protein Sci.</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2005</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Oct</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1110/ps.051473805</style></url></web-urls></urls><number><style face="normal" font="default" size="100%">10</style></number><volume><style face="normal" font="default" size="100%">14</style></volume><pages><style face="normal" font="default" size="100%">2735–2740</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">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.</style></abstract></record></records></xml>