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The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates
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Journal: Protein Sci.
Year: 2004
Volume: 13
Issue: 7
Pages: 1939-1941
DOI: 10.1110/ps.04663504
Type of Publication: Journal Article
Keywords:
Alzheimer Disease; Amino Acids; Animals; Computer Simulation; Humans; Prions; Protein Conformation; Protein Folding; Proteins; Thermodynamics
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.