Abstract
Ribosomal translation includes three main reactions: codon-dependent binding of aminoacyl-tRNA, transpeptidation, and translocation (Fig. 32.1). Cotranslational folding of a nascent peptide also takes place on the ribosome. None of these processes have been studied on the detailed molecular level in terms of molecular kinematics and concrete atomic interactions. At the same time, the atomic structure of tRNA, the principles of tRNA-codon interactions, the chemistry of transpeptidation reactions, and certain restrictions imposed by the ribosome are known. Using this knowledge and accepting some reasonable postulates, the ribosomal processes can be studied by means of molecular models. Some results of the stereochemical modeling experiments are briefly given below.
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Spirin, A.S., Lim, V.I. (1986). Stereochemical Analysis of Ribosomal Transpeptidation, Translocation, and Nascent Peptide Folding. In: Hardesty, B., Kramer, G. (eds) Structure, Function, and Genetics of Ribosomes. Springer Series in Molecular Biology. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-4884-2_32
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DOI: https://doi.org/10.1007/978-1-4612-4884-2_32
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