@article{bibcite_161,
  keywords = {Protein Denaturation, Protein Structure, Secondary, Drug Design, Humans, Amino Acid Sequence, Amyloid, Models, Chemical, Alzheimer Disease, Prions, Parkinson Disease},
  author = {G. G. Tartaglia and A. Cavalli and R. Pellarin and A. Caflisch},
  title = {Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences},
  abstract = {<p>The reliable identification of \&beta;-aggregating stretches in protein sequences is essential for the development of therapeutic agents for Alzheimer{\textquoteright}s and Parkinson{\textquoteright}s diseases, as well as other pathological conditions associated with protein deposition. Here, a model based on physicochemical properties and computational design of \&beta;-aggregating peptide sequences is shown to be able to predict the aggregation rate over a large set of natural polypeptide sequences. Furthermore, the model identifies aggregation-prone fragments within proteins and predicts the parallel or anti-parallel \&beta;-sheet organization in fibrils. The model recognizes different \&beta;-aggregating segments in mammalian and nonmammalian prion proteins, providing insights into the species barrier for the transmission of the prion disease.</p>},
  year = {2005},
  journal = {Protein Science},
  volume = {14},
  pages = {2723-2734},
  month = {2005 Oct},
  issn = {0961-8368},
  doi = {10.1110/ps.051471205},
  language = {eng},
}