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Organism complexity anti‐correlates with proteomic β‐aggregation propensity
Author(s) -
Tartaglia Gian Gaetano,
Pellarin Riccardo,
Cavalli Andrea,
Caflisch Amedeo
Publication year - 2005
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.051473805
Subject(s) - proteome , organism , computational biology , longevity , protein folding , biology , protein aggregation , chemistry , biophysics , bioinformatics , biochemistry , genetics
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.