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

TitleThe role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates.
Publication TypeJournal Article
Year of Publication2004
AuthorsTartaglia GG, Cavalli A, Pellarin R, Caflisch A
JournalProtein Sci.
Volume13
Pagination1939–1941
Date PublishedJul
Abstract

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.

URLhttp://dx.doi.org/10.1110/ps.04663504
DOI10.1110/ps.04663504