Protein synthesis, translation

protein synthesis
ribosome and its part
translation/ protein synthesis
activation of tRNA
steps in translation
release factor
initiation, elongaton and termination

1. PROTEIN SYNTHESIS (TRANSLATION) By – Dr R. K. UPADHYAY PGT, BIOLOGY

2. Proteins are polypeptide. Amino acids are monomer of proteins. Peptide chain are formed in between amino group of one amino acid and carboxylic group of another amino acid. First amino acid is M ethionine . PROTEIN

3. RIBOSOME SITE OF PROTEIN SYNTHESIS

4. Activation of t RNA (Formation of amino acyl t RNA) INITIATION ELONGATION TERMINATION STEPS

5. (Formation of amino acyl t RNA) Activation of t RNA

6. ACTIVATION OF tRANSFER RNA Attachment of amino acid with t RNA Formation of aminoacyl t RNA Aminoacyl t RNA binds with mRNA Enzyme- amino acyl synthetase

7. Small ribosomal unit binds to m RNA and moves Ribosome binds on initiation codon AUG. AUG codes for Methionine . Now larger subunit of ribosome also bind Formation of initiation complex INITIATION

8. Another amino acyl tRNA binds on A site of ribosome Peptide formation takes place in between adjacent amino acids of A and P site ELONGATION

9. After peptide bond formation , ribosome moves at a distance of one codon The A site amino acid with peptide bons move into P site A site is ready to receive new Amino acyl tRNA This step continues and peptide bond formation also continues This result in formation of polypeptide. ELONGATION

10. When ribosome reaches to any of the STOP codons (UAA, UAG, UGA). There is no aminoacyl tRNA for stop codons RF (release factor) bind on ribosome- m RNA complex and dissociate it. Polypeptide releases in cyoplasm TEERMINATION

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