ALPHA-HELIX FORMATION IN C-PEPTIDE RNASE-A INVESTIGATED BY PARALLEL TEMPERING SIMULATIONS
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 | International Journal of Modern Physics C (Q3) | ||
| Dergi ISSN | 0129-1831 Wos Dergi Scopus Dergi | ||
| Dergi Tarandığı Indeksler | SCI-Expanded | ||
| Makale Dili | İngilizce | Basım Tarihi | 01-2007 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 01-01-2007 |
| Cilt / Sayı / Sayfa | 18 / 1 / 91–98 | DOI | 10.1142/S0129183107010292 |
| Makale Linki | http://www.worldscientific.com/doi/abs/10.1142/S0129183107010292 | ||
| UAK Araştırma Alanları |
Yoğun Madde Fiziği
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| 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. |
| Anahtar Kelimeler |
| c-peptide ribonuclease-A | Generalized ensembles | Parallel tempering |
Science Direct
ALPHA-HELIX FORMATION IN C-PEPTIDE RNASE-A INVESTIGATED BY PARALLEL TEMPERING SIMULATIONS
| Atıf Sayıları | |
| Web of Science | 2 |
| Scopus | 2 |
| Google Scholar | 2 |