Prediction of α-Helix Folding of Isolated C-Peptide of Ribonuclease A by Monte Carlo Simulated Annealing
- 1 February 1991
- journal article
- research article
- Published by Oxford University Press (OUP) in Chemistry Letters
- Vol. 20 (2) , 213-216
- https://doi.org/10.1246/cl.1991.213
Abstract
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.Keywords
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