| Literature DB >> 16155201 |
Gian Gaetano Tartaglia1, Riccardo Pellarin, Andrea Cavalli, Amedeo Caflisch.
Abstract
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.Entities:
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Year: 2005 PMID: 16155201 PMCID: PMC2253303 DOI: 10.1110/ps.051473805
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725