BiochemistryAutumn Term – Marlborough SchoolSyllabus Content
• Review of appropriate material from A2 Chemistry – Module 2814 Chains,Rings and Spectroscopy, 5.4.4(e)–(h).• Amino acids, polypeptides and proteins.• Protein structure: primary, secondary, tertiary and quaternary structures.• Denaturation of proteins.
Candidates should be able to:(a) explain the term primary structure of proteins.(b) describe the secondary structure of proteins: α-helix and β-pleated sheet;the stabilisation of these structures by hydrogen bonding.(c) state the importance of the tertiary protein structure and explain itsstabilisation by R groups in the amino acid residues, in terms of ioniclinkages, disulphide bridges, hydrogen bonds and van der Waals’ forces.(d) describe the quaternary structure of proteins, for example: haemoglobinincluding the role of Fe2+.(e) explain denaturation of proteins by heavy metal ions, extremes of temperature and pH changes (see also 5.6.2(d)).