3. PROTEINS C, H, O, N, (S) Polymers made from chains of amino acids 20 amino acids used Linked by a peptide bond

4. In addition fibrous proteins (collagen) form structural components in cells and tissues

6. Amino Acids Central carbon has attached: –Amine group –Acid group –Functional group (R) – determines nature of amino acid R groups fall into 4 categories Non-polar- only carbons; chains or aromatic rings (methionine has sulphur) Uncharged Polar- carbons with amine groups (NH 2 ) or - hydroxyl groups (OH) Acidic- carboxylic acid groups (COOH) ionizes to negative charge COO - Basic- terminal amine groups (not next to C=O) ionizes to NH 3 +

8. Peptide bond Amino acids joined by a peptide bond Condensation reaction between –COOH of 1 st amino acid and NH 2 of 2 nd amino acid Chains are called peptides (short)/ polypeptides (longer) Peptide bond is rigid Bonds either side can rotate –Introduces flexibility allowing proteins to take up variety of shapes.

9. Protein Structure 4 levels –Primary –Secondary –Tertiary –Quaternary

10. PRIMARY STRUCTURE Order in which amino acids are linked together –Written starting at the N (amino) terminus –e.g. –Arg-Lys-Phe-Glu-Ser-Gly- –R K F E S G NC N terminus C terminus

11. SECONDARY STRUCTURE Two possible shapes in the protein chain each stabilised by Hydrogen bonds: –  -pleated sheet –  -helix

12.  -pleated sheet Peptide chains arranged side by side Held together by H-bonds between the two chains Parallel (chains running same direction) N  C Antiparallel (chains in opposite directions) N  C C  N

13.  -pleated sheet Silk –Resistant to stretch (very strong)

14.  -helix Peptide chain coils into a helix –Held by H-bond between N-H group and the C=O 4 residue away 4 residues per turn

15.  -helix Hair/Wool (keratin) –Stretchy (er) –  -helices coiled together to form a superhelix –For horn/hoof more disulphide bridges are present (covalent)

16. Tertiary Structure The overall folded shape of a protein held together by (usually) weak forces. –Hydrogen bonding which doesn’t form secondary structure –Hydrophobic interactions Place non-polar amino acids inside protein Polar amino acids on surface –Van der Waals forces –Ionic interactions (strong) –Disulphide bridges (strong) Covalent bond between cysteine residues Myoglobin

18. With reference to bonding, explain why enzyme activity decreases as you increase the temperature above the optimum, and as you move pH away from the optimum.

19. Proteins fold to take up their shape Shape is determined by primary structure – order of hydrophobic/ hydrophilic amino acids & relative positions of polar/charged amino acids. Loss of tertiary structure is called denaturation.

20. Lysozyme Proteins are 3D

21. Primary structure determines tertiary structure Mutation acid (polar) for non polar changes folding pattern

22. Prosthetic groups Some proteins have permanently bound non protein groups, called prosthetic groups –e.g. myoglobin & haemoglobin bind to a porphyrin (haem) chelating an Iron atom –e.g. Chlorophyll has a similar prosthetic group chelating Mg The protein without its prosthetic group is called an apoprotein, with its group it is called a holoprotein

23. Co-factors/ Co-enzymes Other proteins have inorganic ions temporarily bound to them –E.g. copper/ zinc on enzymes Others have carbon containing molecules temporarily attached –e.g. Coenzyme A, NAD, FAD

24. Quaternary Structure Only present if protein has more than one polypeptide chain Describes the shape adopted by the interacting polypeptide chains

28. Nucleic Acids DNA –Deoxyribonucleic Acid RNA –Ribonucleic Acid Video

29. Nucleic Acids Summary Knowledge –DNA deoxyribose sugar, –RNA ribose sugar –DNA double stranded (antiparallel) –RNA single stranded –DNA thymine, –RNA uracil –A double (hydrogen) bonds to T (A 2 T) –G triple (hydrogen) bonds to C (G 3 C) –G & A purines (small word, big molecule –A Giant) –C,T & U pyrimidines (big word, small molecule)