Proteome-level interplay between folding and aggregation propensities of proteins.
With the advent of proteomics, there is an increasing need of tools for predicting the properties of large numbers of proteins by using the information provided by their amino acid sequences, even in the absence of the knowledge of their structures. One of the most important types of predictions concerns whether proteins will fold or aggregate. Here, we study the competition between these two processes by analyzing the relationship between the folding and aggregation propensity profiles for the human and Escherichia coli proteomes. These profiles are calculated, respectively, using the CamFold method, which we introduce in this work, and the Zyggregator method. Our results indicate that the kinetic behavior of proteins is, to a large extent, determined by the interplay between regions of low folding and high aggregation propensities.
Tartaglia
Gian Gaetano
GG
Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK. gian.tartaglia@crg.es
Vendruscolo
Michele
M
D019295:Computational Biology / Q000379:methods; D004926:Escherichia coli; D029968:Escherichia coli Proteins / Q000378:metabolism*; D006801:Humans; D011485:Protein Binding; D011489:Protein Denaturation; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*; D020543:Proteome; D040901:Proteomics / Q000379:methods
D029968:Escherichia coli Proteins; D011506:Proteins; D020543:Proteome