Monte Carlo simulation study of melittin: protein folding and temperature dependence
Yazarlar (3)
Prof. Dr. Majıd MONAJJEMI Islamic Azad University, Science And Research Branch, İran
S. Ketabi
University of Tehran, İran
University of Tehran, İran
A. Amiri
Islamic Azad University, İran
Islamic Azad University, İran
| Makale Türü | Özgün Makale (SSCI, AHCI, SCI, SCI-Exp dergilerinde yayınlanan tam makale) | ||
| Dergi Adı | Russian Journal of Physical Chemistry A (Q4) | ||
| Dergi ISSN | 0036-0244 Dergi Bilgileri (2006) | ||
| Makale Dili | İngilizce | Basım Tarihi | 11-2006 |
| Cilt / Sayı / Sayfa | 80 / 1 / – | DOI | 10.1134/S0036024406130103 |
| Makale Linki | http://www.scopus.com/inward/record.url?eid=2-s2.0-33750981827&partnerID=MN8TOARS | ||
| UAK Araştırma Alanları |
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| Özet |
| The tetramerization of melittin, a 26-amino-acid peptide, is considered as a model for protein folding. The Monte Carlo simulation was used to study the folding arrangement of melittin, and the results are compared with the experiment. An acceptance rate of 50% for new configurations is achieved by using ranges of ±0.001 Å for the translations and ±15°C for the rotations. Around 311 K, the folded structure of the protein has the greatest stability; the range from -40 to -80 shows the best φ angles for melittin. The final optimized structure of melittin strongly depends on the temperature. The melittin tetramer is found to have a temperature of maximum stability ranging from 35.5 to 43°C. © Nauka/Interperiodica 2006. |
| Anahtar Kelimeler |
BM Sürdürülebilir Kalkınma Amaçları
| Atıf Sayıları | |
| Web of Science | 35 |
| Scopus | 85 |