Secondary structure prediction of beta-hairpin peptide tryptophan zipper-I
Yazarlar (2)
Prof. Dr. Gökhan GÖKOĞLU Karabük Üniversitesi, Türkiye
Tarık Çelik Turkish Academy Of Sciences, Türkiye
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Physica A Statistical Mechanics and Its Applications (Q2) | ||
| Dergi ISSN | 0378-4371 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 06-2008 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 01-06-2008 |
| Cilt / Sayı / Sayfa | 387 / 14 / 3537–3545 | DOI | 10.1016/j.physa.2008.02.065 |
| Makale Linki | https://linkinghub.elsevier.com/retrieve/pii/S037843710800246X | ||
| UAK Araştırma Alanları |
Yoğun Madde Fiziği
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| Özet |
| We 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. |
| Anahtar Kelimeler |
| β-hairpin | Generalized ensembles | Simulated tempering | Tryptophan zipper |