Folding and aggregation of designed proteins.

@article{Broglia1998FoldingAA,
  title={Folding and aggregation of designed proteins.},
  author={Ricardo A. Broglia and Guido Tiana and Samuela Pasquali and H. Eduardo Roman and E. Vigezzi},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1998},
  volume={95 22},
  pages={
          12930-3
        }
}
  • R. Broglia, G. Tiana, E. Vigezzi
  • Published 14 April 1998
  • Chemistry
  • Proceedings of the National Academy of Sciences of the United States of America
Protein aggregation is studied by following the simultaneous folding of two designed identical 20-letter amino acid chains within the framework of a lattice model and using Monte Carlo simulations. It is found that protein aggregation is determined by elementary structures (partially folded intermediates) controlled by local contacts among some of the most strongly interacting amino acids and formed at an early stage in the folding process. 
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