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Nano theoretical studies of fMet-tRNA structure in protein synthesis of prokaryotes and its comparison with the structure of fAla-tRNA   
Yazarlar (4)
Dr. Öğr. Üyesi Fatemeh MOLLAAMIN Dr. Öğr. Üyesi Fatemeh MOLLAAMIN
M. Noei
M. Monajjemi
R. Rasoolzadeh
Devamını Göster
Özet
It is generally accepted that initiation of protein synthesis in Escherichia coli starts with formyl-methionine, directed by the codons AUG or GUG. Protein synthesis proceeds by transfer of the growing polypeptide chain from the tRNA bound to the ribosomal P site to the incoming aminoacyl-tRNA in the adjacent A site. After translocation of the ribosome in the 30 direction of the mRNA, by the action of elongation factor G, the A site again becomes empty and the next codon exposed so that a new aminoacyl-tRNA ternary complex can be selected (Ogle and Ramakrishnan, 2005).Synthetic polynucleotide containing AUG and/or GUG codons as well as natural mRNA have been used extensively in order to elucidate the mechanism of initiation of protein synthesis (Grunberg-Manago, 1977). In all these studies it has been assumed that binding of fMet-tRNA to ribosome’s is the polynucleotide in bacteria the start codon AUG is recognized by fMet-tRNA. This tRNA does not recognize internal AUG codons. Initiation of protein biosynthesis requires the correct positioning of charged initiator tRNA, fMet-tRNA in the ribosomal P-site of the mRNA-programmed 70S ribosome’s (Gualerzi and Pon, 1990; La Teana et al., 1996; Monajjemi et al., 2008; Spurio et al., 1993; Forster et al., 1999). The rapid development of molecular biology in recent years has been mirrored by the rapid development of
Anahtar Kelimeler
Natural bond orbital (NBO) | fMet-tRNA | NMR | Opt | SCRF | fAla-tRNA
Makale Türü Özgün Makale
Makale Alt Türü ESCI dergilerinde yayınlanan tam makale
Dergi Adı AFRICAN JOURNAL OF MICROBIOLOGY RESEARCH
Dergi ISSN 1996-0808
Dergi Tarandığı Indeksler
Makale Dili İngilizce
Basım Tarihi 09-2011
Cilt No 5
Sayı 18
Sayfalar 2667 / 2674
Atıf Sayıları
WoS 19
Google Scholar 19

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