The role of initiator tRNA I met in fidelity of initiation of protein synthesis

Monajemi, H. and Abdullah, W.A.T.W. and Zain, Sharifuddin Md and Daud, M.N. and Omar, N.Y.M. (2011) The role of initiator tRNA I met in fidelity of initiation of protein synthesis. Nucleosides, Nucleotides and Nucleic Acids, 30 (9). pp. 726-739. ISSN 15257770, DOI https://doi.org/10.1080/15257770.2011.605780.

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Abstract

The proper arrangement of amino acids in a protein determines its proper function, which is vital for the cellular metabolism. This indicates that the process of peptide bond formation requires high fidelity. One of the most important processes for this fidelity is kinetic proofreading. As biochemical experiments suggest that kinetic proofreading plays a major role in ensuring the fidelity of protein synthesis, it is not certain whether or not a misacylated tRNA would be corrected by kinetic proofreading during the peptide bond formation. Using 2-layered ONIOM (QM/MM) computational calculations, we studied the behavior of misacylated tRNAs and compared the results with these for cognate aminoacyl-tRNAs during the process of peptide bond formation to investigate the effect of nonnative amino acids on tRNAs. The difference between the behavior of initiator tRNA i met compared to the one for the elongator tRNAs indicates that only the initiator tRNA i met specifies the amino acid side chain. Copyright © Taylor and Francis Group, LLC.

Item Type: Article
Funders: UNSPECIFIED
Additional Information: Department of Chemistry, Faculty of Science Building, University of Malaya, 50603 Kuala Lumpur, MALAYSIA
Uncontrolled Keywords: ONIOM, peptide bond formation, ribosome, tRNA, amino acid, aminoacyl transfer RNA, transfer RNA, methionine transfer RNA,, protein, article, electron transport, molecular mechanics, protein binding, protein function, protein structure, protein synthesis, quantum mechanics, RNA structure, chemistry, genetics, metabolism, RNA translation, X ray crystallography, Crystallography, X-Ray, Peptide Chain Initiation, Translational, Protein Biosynthesis, Proteins, Ribosomes, RNA, Transfer, Met RNA, Transfer, Met
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science > Department of Chemistry
Depositing User: Miss Malisa Diana
Date Deposited: 13 May 2013 02:07
Last Modified: 25 Oct 2019 09:09
URI: http://eprints.um.edu.my/id/eprint/6065

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