Molecular dynamic and monte carlo study on nanoenergetic binding sites of neuraminidase in different media
Yazarlar (4)
| Makale Türü |
Özgün Makale
(SCOPUS dergilerinde yayınlanan tam makale)
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| Dergi Adı | AFRICAN JOURNAL OF MICROBIOLOGY RESEARCH | ||
| Dergi ISSN | 1996-0808 Dergi Bilgileri (2012) | ||
| Dergi Tarandığı Indeksler | |||
| Makale Dili | İngilizce | Basım Tarihi | 02-2012 |
| Kabul Tarihi | – | Yayınlanma Tarihi | 29-02-2012 |
| Cilt / Sayı / Sayfa | 6 / 8 / 1713–1717 | DOI | 10.5897/AJMR11.930 |
| Makale Linki | https://academicjournals.org/article/article1380296102_Monajjemi%20et%20al.pdf | ||
| UAK Araştırma Alanları |
Fen Bilimleri ve Matematik
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| Özet |
| Influenza panedemic affect 25 to 30% of the world's population. Neuraminidase (NA) is the most important surfase glycoprotein of the virus causing cleavage of the sialic acid moieties and releasing of newly formed viral particles. The active site of NA is highly conserved all subtype of influaenza virus, then Neuraminidase is the target of drug designs. Using molecular dynamic (MD) and Monte Carlo simulatory methods, the NA structure and its stability different dielcteric (vacuum, water and methanol) and different tempeartures (298, 310, 315, 329 and 333K) was assessed. Measurements of potential energy (Kcal/mol) of binding sites NA in different dielectrics and in different temperatures revealed that at time step size 0 ps, drug binding sites have maximum energy level, and at time step size 100 ps, have minimum energy level and maximum stability. |
| Anahtar Kelimeler |
| Neuraminidase | influenza | molecular dynamic | binding sit | free energy | dielectric |
BM Sürdürülebilir Kalkınma Amaçları
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| Web of Science | 2 |
| Google Scholar | 4 |