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]

Organism complexity anti-correlates with proteomic β-aggregation propensity

Tartaglia G. G.;
2005

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. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society.
2005
Aggregation; Intrinsically disordered proteins; Protein aggregation propensity; Proteome; Amino Acid Sequence; Animals; Databases, Protein; Longevity; Protein Conformation; Protein Denaturation; Proteins; Models, Molecular; Protein Folding; Proteome
01 Pubblicazione su rivista::01a Articolo in rivista
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]
File allegati a questo prodotto
File Dimensione Formato  
Tartaglia_Organism_2005.pdf

accesso aperto

Tipologia: Versione editoriale (versione pubblicata con il layout dell'editore)
Licenza: Tutti i diritti riservati (All rights reserved)
Dimensione 339.73 kB
Formato Adobe PDF
339.73 kB Adobe PDF

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/1452096
Citazioni
  • ???jsp.display-item.citation.pmc??? 16
  • Scopus 36
  • ???jsp.display-item.citation.isi??? 31
social impact