Prediction of α-Helix Folding of Isolated C-Peptide of Ribonuclease A by Monte Carlo Simulated Annealing

Conformation of the C-peptide fragment of RNase A is calculated by Monte Carlo simulated annealing. Starting from completely random initial conformations and minimizing the total potential energy without any bias, we obtained partial α-helix structure with a high probability (≈ 40%). The energetically most favourable structure exhibits a 2.5-turn α-helix. The results of simulation are consistent with the experimental implication for the role of charged residues for α-helix stability in this peptide.