Abstract
We have carried out Monte Carlo simulations to predict tertiary structure of a few peptides with the use of simulated annealing. The simulation is made in a completely unrestricted manner using generic potential energy parameters determined for each amino acid as input. For the isolated C-peptide fragment of ribonuclease A we found that the α-helix appears close to the ground state of this peptide in agreement with the indication from the experiment. We have also succeeded in reproducing the α-helix propensity for several amino acid residues in homopolymer simulations.
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