| Yazarlar (2) |
Prof. Dr. Gökhan GÖKOĞLU
Karabük Üniversitesi, Türkiye |
Tarık Çelik
Türkiye |
| Özet |
| We have performed parallel tempering simulations of a 13-residue peptide fragment of ribonuclease-A, c-peptide, in implicit solvent with constant dielectric permittivity. This peptide has a strong tendency to form α-helical conformations in solvent as suggested by circular dichroism (CD) and nuclear magnetic resonance (NMR) experiments. Our results demonstrate that 5th and 8-12 residues are in the α-helical region of the Ramachandran map for global minimum energy state in solvent environment. Effects of salt bridge formation on stability of α-helix structure are discussed. © World Scientific Publishing Company. |
| Anahtar Kelimeler |
| c-peptide ribonuclease-A | Generalized ensembles | Parallel tempering |
| Makale Türü | Özgün Makale |
| Makale Alt Türü | SSCI, AHCI, SCI, SCI-Exp dergilerinde yayımlanan tam makale |
| Dergi Adı | INTERNATIONAL JOURNAL OF MODERN PHYSICS C |
| Dergi ISSN | 0129-1831 Wos Dergi Scopus Dergi |
| Dergi Tarandığı Indeksler | SCI-Expanded |
| Dergi Grubu | Q3 |
| Makale Dili | İngilizce |
| Basım Tarihi | 01-2007 |
| Cilt No | 18 |
| Sayı | 1 |
| Sayfalar | 91 / 98 |
| Doi Numarası | 10.1142/S0129183107010292 |
| Makale Linki | http://www.worldscientific.com/doi/abs/10.1142/S0129183107010292 |
