Gökoǧlu G.Çelik, T.2016-02-082016-02-0820080378-4371http://hdl.handle.net/11693/23110We have investigated the folding properties of tryptophan zipper-I molecule which folds into a stable β-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 β-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. © 2008 Elsevier Ltd. All rights reserved.Englishβ-hairpinGeneralized ensemblesSimulated temperingTryptophan zipperAlgorithmsHydrogenMolecular structureNuclear magnetic resonanceGeneralized ensemblesSimulated temperingTryptophan zipperPeptidesArticle10.1016/j.physa.2008.02.065