title: Basin hopping simulations for all-atom protein folding.
abstract: We investigate different protocols of the basin hopping technique for de novo protein folding. Using the protein free-energy force field PFF01 we report the reproducible all-atom folding of the 20-amino-acid tryptophan-cage protein [Protein Data Bank (PDB) code: 112y] and of the recently discovered 26-amino-acid potassium channel blocker (PDB code: 1wqc), which exhibits an unusual fold. We find that simulations with increasing cycle length and random starting temperatures perform best in comparison with other parametrizations. The basin hopping technique emerges as a simple but very efficient and robust workhorse for all-atom protein folding.
authors.affiliation: Forschungszentrum Karlsruhe GmbH, Institut für Wissenschaftliches Rechnen, Postfach 3640, D-76021 Karlsruhe, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Verma
authors.forename: A
authors.initials: A
authors.lastname: Schug
authors.forename: K H
authors.initials: KH
authors.lastname: Lee
authors.forename: W
authors.initials: W
authors.lastname: Wenzel
mesh_terms: D003198:Computer Simulation; D010455:Peptides / Q000737:chemistry*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013816:Thermodynamics
chemical_list: D010455:Peptides; C508725:Trp-cage peptide