The Mechanism by Which Ribosomes Form Proteins

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The objective is to understand in chemical-mechanical terms how ribosomes and the macromolecules that interact with them form proteins. The primary objective is to monitor and describe the extension of a nascent peptide as it is extended by the stepwise addition of amino acids at the ribosomal peptidyl transferase center. particular attention will be given to the question of whether the nascent peptide is channeled from the peptidyl transferase to the exit domain through a tunnel that transversed the large ribosomal subunit, and if so, to determine how the nascent peptide is inserted into the tunnel. Secondary objective are to determine when the mRNA moves through the ribosome during the reaction step of peptide elongation and to further analyze how antibiotics such as erythromycin and chloromphenical inhibit protein synthesis. The approach is to covalently attack fluorophores at specific sites on the tRNA, mRNA ribosomal proteins, and ribosomal RMA, then to use fluorescence techniques to monitor changes in the position and conformation of the components that occur during the specific reaction steps of protein synthesis. The results are anticipated to be directly relevant to the in vitro synthesis of artificial enzymes by biotechnological procedures and to the control of protein synthesis in certain pathologies.