@article{bibcite_100,
  keywords = {Computer Simulation, Protein Folding, Thermodynamics, Animals, Humans, Protein Conformation, Proteins, Alzheimer Disease, Amino Acids, Prions},
  author = {G. G. Tartaglia and A. Cavalli and R. Pellarin and A. Caflisch},
  title = {The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates},
  abstract = {<p>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.</p>},
  year = {2004},
  journal = {Protein Science},
  volume = {13},
  pages = {1939-1941},
  month = {2004 Jul},
  issn = {0961-8368},
  doi = {10.1110/ps.04663504},
  language = {eng},
}