Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
974945 | Physica A: Statistical Mechanics and its Applications | 2008 | 9 Pages |
We have investigated the folding properties of tryptophan zipper-I molecule which folds into a stable ββ-hairpin motif in aqueous solution as suggested by nuclear magnetic resonance (NMR) experiments. An all-atom presentation, including hydrogen, was used with an implicit solvent. As a simulation technique, simulated tempering algorithm was used to obtain equilibrium conformations of the molecule at ten distinct temperatures. Our minimum energy configuration obtained from simulated tempering algorithm is a ββ-hairpin motif with 1.30 Å backbone root-mean-square deviation from the reference PDB structure (1le0.pdb). Several quantities and exhaustive folding free energy landscapes were determined and discussed in order to clarify the folding behavior.