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G.G. Tartaglia; A. Cavalli; R. Pellarin; A. Caflisch

Journal: Protein Sci.
Year: 2004
Volume: 13
Issue: 7
Pages: 1939-1941
DOI: 10.1110/ps.04663504
Type of Publication: Journal Article

Alzheimer Disease; Amino Acids; Animals; Computer Simulation; Humans; Prions; Protein Conformation; Protein Folding; Proteins; Thermodynamics


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.