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              Biopolymers                                                                                 239









































                     FIGURE 22 Elongation of a peptide chain. (I, on the serine t-RNA, signifies inosine, a base similar in structure to
                     guanine, but lacking the NH 2 group. Inosine is common at t-RNA anticodons, and can pair with U, C, or A on a codon.)

              free t-RNA moves to the E-site. A shape change at the ri-  synthesis to help ensure correct initiation, elongation, and
              bosome surface and binding of a new amino-acyl-t-RNA  termination of the chain. After synthesis, many proteins
              at the A site cause the free t-RNA to drop out of the E-site.  undergo further modifications—amino acid side chains
              The processes shown in Fig. 22 can now be repeated over  may be altered, segments of polypeptide chain may be
              and over, to give a growing polypeptide chain. In this case,  removed, or prosthetic groups may be added.
              the third amino acid to be joined to the protein would be  Protein biosynthesis must at all times be under strict
              asparagine.                                       control. Much of this control, particularly in bacteria, is
                A ribosome moves along the m-RNA until a terminator  exerted at the level of transcription (i.e., production of
              codon appears at the A-site. The completed polypeptide  m-RNA). In some cases, a protein known as a repres-
              chain is released from the last t-RNA, the t-RNA dissoci-  sor recognizes and binds to a segment of DNA close to
              ates from the ribosome, and the ribosome itself splits into  a site for initiation of m-RNA synthesis. The repressor
              two subunits ready to recommence protein synthesis.  binds in the grooves of the DNA helix and effectively pre-
                The whole process, whereby a sequence of bases on m-  vents biosynthesis of the m-RNA. When that m-RNA is
              RNA becomes an amino acid sequence of a polypeptide  required, a shape-change can be brought about in the re-
              chain, is called translation, and is much more complex  pressor protein by another molecule called an inducer; the
              than presented here. The ribosome plays an active part in  repressor no longer binds to the DNA and transcription of
              the process and minor changes in its structure may occur  m-RNAcantakeplace.Inotherinstances,specificproteins
              at more than one stage of protein synthesis. Ribosome  can bind to DNA and enhance the synthesis of particular
              structure is more complicated than depicted in Figs. 21 and  m-RNA molecules. Translational control is also possible.
              22; a cavity exists between the two subunits in the intact  Alterations in protein initiation factors or binding of pro-
              ribosome, and it is in this cavity that the t-RNAs can bind.  teins to m-RNA to alter its secondary structure or mask
              In addition, many protein factors are involved in protein  theinitialribosomerecognitionsitecanchangetheamount
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