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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(More)
The stability of model proteins with designed sequences is assessed in terms of the number of sequences (obtained from the designed sequence through mutations), which fold into the " native " conformation. By a complete enu-meration of the total number of sequences obtained by introducing up to 4 point mutations and up to 7 composition–conserving mutations(More)
  • G Potel, B F Bayman, +4 authors Broglia
  • 2009
Arguably, the greatest achievement of many–body physics in the fifties was that of developing the tools for a complete description and a thorough understanding of superconductivity in metals. At the basis of it one finds BCS theory and the Josephson effect. The first recognized the central role played by the appearance of a macroscopic coherent field(More)
We study the impact of mutations (changes in amino acid sequence) on the thermodynamics of simple protein-like heteropolymers consisting of N monomers, representing the amino acid sequence. The sequence is designed to fold into its native conformation on a cubic lattice. It is found that quite a large fraction, between one half and one third of the(More)
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