Volume 59, Number 5, September 2002
|Page(s)||721 - 727|
|Section||Condensed matter: structure, mechanical and thermal properties|
|Published online||01 September 2002|
Folding dynamics of the helical structure observed in a minimal model
Department of Physics, University of Waterloo - Waterloo, Ontario, NZN 3G1 Canada
Accepted: 5 June 2002
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.
PACS: 64.60.Cn – Order-disorder transformations; statistical mechanics of model systems / 87.15.By – Structure and bonding / 64.70.Kb – Solid-solid transitions
© EDP Sciences, 2002
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