Folding dynamics of the helical structures in a minimal model

Details Folding dynamics of the helical structures in a minimal model Folding dynamics of the helical structures in a minimal model

2002-01-21

arxiv.org/abs/cond-mat/0201374v1

Revised version can be seen: Europhys Lett 59, 721 (2002)

Physics

Condensed Matter

Soft Condensed Matter

3 figures Submitted to Europhys Letter

Scientific paper

10.1209/epl/i2002-00185-0

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.

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