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Folding of Proteins with Diverse Folds

Sandipan Mohanty ^* and Ulrich H. E. Hansmann ^* 

^* John von Neumann Institut für Computing, Forschungszentrum Jülich, Jülich, Germany; and Department of Physics, Michigan Technological University, Houghton, Michigan

Correspondence: Address reprint requests to U. H. E. Hansmann, Tel.: 906-487-4552; E-mail: hansmann{at}mtu.edu.

Using parallel tempering simulations with high statistics, we investigate the folding and thermodynamic properties of three small proteins with distinct native folds: the all-helical 1RIJ, the all-sheet beta3s, and BBA5, which has a mixed helix-sheet fold. In all three cases, simulations with our energy function find the native structures as global minima in free energy at experimentally relevant temperatures. However, the folding process strongly differs for the three molecules, indicating that the folding mechanism is correlated with the form of the native structure.

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