Folding dynamics of the helical structure observed in a minimal model

The folding of a polypeptide is associated with the formation of domain structures that have the form of α-helix or β-sheet. Of biological importance is how a secondary structure, such as an α-helix, spontaneously forms during the collapse of a peptide from an initial denatured state. The Monte Carlo implementation of a recent helix-forming model enables us to study the entire folding process dynamically. As shown by our computer simulations, the foldability and helical propagation are both strongly correlated to the nucleation properties of a given residue sequence