Journal
PROTEIN SCIENCE
Volume 13, Issue 7, Pages 1939-1941Publisher
WILEY
DOI: 10.1110/ps.04663504
Keywords
amyloid; prion; aggregation rate; Alzheimer; protein deposit; mutation
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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.
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