The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates.
|Title||The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates.|
|Publication Type||Journal Article|
|Year of Publication||2004|
|Authors||Tartaglia GG, Cavalli A, Pellarin R, Caflisch A|
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.