1. Amino acids and proteins Section 13.10 (pages 326-329)

2. Amino acids Amino acids contain at least one amino group and one carboxylic acid group (they are an example of bifunctional compounds) α-amino acids are particularly important in living systems. α-carbon

3. Naming the amino acids Amino acids are usually referred to by their trivial names as this is usually shorter than the systematic name. (see sheet)

4. Thinking about amino acids We’ve just said that they have (generally) one amino group and one carboxylic acid. What can you tell me about each of these functional groups? The amino group is basic. The carboxylic acid is acidic.

5. A quick recap on acids and bases We think of them as proton acceptors and donators.

6. Thinking about amino acids So what? The ends can react with each other and we get : This is called a zwitterion (the name for a particle containing both +ve and –ve charged groups)

7. Physical properties of amino acids Have you ever seen a sample of amino acids? They are crystalline solids They area also highly soluble in water because they are effectively ionic And (unless there is another ‘ionisable group’) they are neutral in aqueous solution

8. Amino acids in solution They form what we call ‘buffer’ solutions. (?) A buffer solution is a solution that can withstand the addition of small amounts of acid or alkali with little change to the pH. HO - + H 3 N + -CHR-COO -  H 2 O + H 2 N-CHR-COO - H 3 O + + H 3 N + -CHR-COO -  H 2 O + H 3 N + -CHR-COOH

9. Peptides (or poly peptides) An amines can react with a carboxylic acid to form a secondary amide. Water is eliminated so this is a condensation reaction When this happens between amino acids we call the secondary amide group a peptide link

10. The structure of proteins The Primary structure is the unique sequence of amino acids (residues). Most proteins have a precise shape Secondary structure refers to the initial folding. Two common arrangements are sheets and helices

11. The (α) helix Each carbonyl (C=O) forms a hydrogen bond with an N-H group 4 peptide links along.

12. The (β- pleated) sheet Chains lying along side each other

13. Tertiary structure After regions of secondary structure have formed many proteins fold further to give their final shape, the tertiary structure. As well as Hydrogen bonds the following are also very important Instantaneous dipole-induced-dipole Ionic bonds Covalent bonding

14. Hydrolysis This can be done by heating in in a moderately concentrated acid or alkali solution In living organisms this hydrolysis is catalysed by enzymes Chromatography can be used to identify individual amino acids present in a polypeptide.

15. Summary Amino acids exist as zwitterions. Protein structure has three levels. There are four kinds of bonding involved in protein structure: what are they?