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© Research
Publication : Protein science : a publication of the Protein Society

The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates

Team: Structural Bioinformatics
Member: Riccardo Pellarin
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Protein science : a publication of the Protein Society - 28 May 2004

Tartaglia GG, Cavalli A, Pellarin R, Caflisch A

Link to Pubmed [PMID] – 15169952

Protein Sci. 2004 Jul;13(7):1939-41

The mechanisms by which peptides and proteins form ordered aggregates are not well understood. Here we focus on the physicochemical properties of amino acids that favor ordered aggregation and suggest a parameter-free model that is able to predict the change of aggregation rates over a large set of natural sequences. Furthermore, the results of the parameter-free model correlate well with the aggregation propensities of a set of peptides designed by computer simulations.