Monajemi, Hadieh and M. Zain, Sharifuddin and Wan Abdullah, Wan Ahmad Tajuddin (2021) A new step in kinetic proofreading due to misacylated-tRNA during ribosomal peptide bond formation. Nucleosides, Nucleotides and Nucleic Acids, 40 (6). pp. 635-646. ISSN 1525-7770, DOI https://doi.org/10.1080/15257770.2021.1923742.
Full text not available from this repository.Abstract
The translational accuracy in protein synthesis is contributed to by several mechanisms in the ribosome, generally called kinetic proofreading. This process in the ribosome inhibits the non-cognate codon-anticodon interaction. However, it is not sufficient for fidelity of protein synthesis since a wrong amino acid can easily be added to the growing polypeptide chain if a tRNA while cognate to the mRNA, carries a non-cognate amino acid. Therefore, additional to the kinetic proofreading, there must be some hitherto unknown characteristic in misacylated-tRNAs to stop the process of protein synthesis if such misacylated-tRNA is accommodated in the ribosomal A-site. In order to understand this characteristic, we have performed computational quantum chemistry analysis on five different tRNA molecules, each one attached to five different amino acids with one being cognate to the tRNA and the other four non-cognate. This study shows the importance of aminoacyl-tRNA binding energy in ensuring fidelity of protein synthesis.
| Item Type: | Article |
|---|---|
| Funders: | UNSPECIFIED |
| Uncontrolled Keywords: | ONIOM; QM; MM; DFT; Aminoacyl-tRNA; Ribosome; Protein synthesis |
| Subjects: | Q Science > QC Physics Q Science > QD Chemistry |
| Divisions: | Faculty of Science > Department of Chemistry Faculty of Science > Department of Physics |
| Depositing User: | Ms Zaharah Ramly |
| Date Deposited: | 25 May 2022 04:15 |
| Last Modified: | 25 May 2022 04:15 |
| URI: | http://eprints.um.edu.my/id/eprint/27146 |
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