  The folding of a polypeptide is an example of the cooperative effects of the
amino-acid residues. Of recent interest is how a secondary structure, such as a
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 the computer simulations, the foldability and helical propagation
are both strongly correlated to the nucleation properties of the sequence.
