COMPUTER-SIMULATIONS OF DE-NOVO DESIGNED HELICAL PROTEINS

In the context of reduced protein models, Monte Carlo simulations of t hree de novo designed helical proteins (four;member helical bundle) we re performed, At low temperatures, for all proteins under consideratio n, protein-like folds having different topologies were obtained from r andom starting conformations. These simulations are consistent with ex perimental evidence indicating that these de novo designed proteins ha ve the features of a molten globule state. The results of Monte Carlo simulations suggest that these molecules adopt four-helix bundle topol ogies. They also give insight into the possible mechanism of folding a nd association, which occurs in these simulations by on-site assembly of the helices, The low-temperature conformations of all three sequenc es have the features of a molten globule state.