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 G.G, Cavalli A., Pellarin R., Caflisch A. |
| Journal | Protein Science |
| Volume | 13 |
| Issue | 7 |
| Pagination | 1939-1941 |
| Date Published | 2004 Jul |
| Type of Article | Research 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. |
| DOI | 10.1110/ps.04663504 |
| pubindex | 0058 |
| Alternate Journal | Protein Sci. |
| PubMed ID | 15169952 |
| PubMed Central ID | PMC2279921 |
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