ANHB1101 Final: Embryogenesis_Folding

• School: UWA
• Department: Anatomy and Human Biology/Anatomy, Physiology and Human Biology
• Course: ANHB1101
• Professor: Julie Hill

Document Summary

Shape and structure of protein specifies function of protein peptide bonds form between amino group and carboxyl group cumulative r group determines the property of polypeptide solubility is thermodynamically favorable hydrophilic molecule: can hydrogen bond with water and are charge polarized hydrophobic molecule: can not hydrogen bond and are not polarized amino acids that have hydrophobic chains are nonpolar and these a. a tends to be in the interior of soluble proteins. Special amino acids cysteine forms covalent bonds with other cysteine molecules by making disulphide bridges glycine (1 h) allows bends in the polypeptide chain proline: side chain forms bond with amine part of amino acid causing kink histidine: amino diethyl side chain shifts from charged to uncharged peptide bonds form through condensation reaction translation occurs in ribosome: copy of rna goes to outer part of cell ribosomes translate genetic information in rna to amino acids that would become proteins transfer molecules bring amino acids to ribosome.