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Lecture 16

BIO206 Lecture 16 Chapter 7.pdf

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George S Espie

Lecture 16/ Chapter 7 November-06-13 11:51 AM - see here what happens at termination peptidyl transferase becomes a hydrolase enzyme - water “attacks” bond between peptide and tRNA, the 3’OH of the tRNA is released and the rest of the water molecule becomes part of the C terminus carboxyl group of the peptide. - when the peptide is released if it hasn’t already started to it will fold into its 3D conformation (may have CHAPERONES helping) - there is a “latch” holding the domains of the protein together - when GTP is bound this latch is closed, and the tRNA binds to the ribosome with the help of the factor - the hydrolysis of GTP to GDP causes a small conformational change (only a few H atoms movement) but this is magnified by subsequent shifts throughout the protein - the “latch” is released and subunits can twist apart - tRNA is released and is free to be ejected later • GDP release with the help of other elongation factors EF-Ts and GTP binding ready EF-Tu for the next tRNA, and protein synthesis proceeds • But there is a spontaneous movement of the aminoacyl ends of the tRNAs relative to the 50S subunit, resulting in peptidyl-tRNA in a P/A hybrid site (P in the large ribosomal subunit but A in the small subun
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