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The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates
Author(s) -
Tartaglia Gian Gaetano,
Cavalli Andrea,
Pellarin Riccardo,
Caflisch Amedeo
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.04663504
Subject(s) - dipole , moment (physics) , aromaticity , chemistry , chemical physics , biological system , computational chemistry , protein aggregation , statistical physics , physics , biology , molecule , biochemistry , classical mechanics , organic chemistry
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.