1. What is they, what makes them etc
Proteins
What is they, what makes them etc

2. Proteins are polymers
In other words they are lots and lots of monomers
This is different than Carbohydrates and Lipids because the monomers are all very different and this leads to variation in behaviour and structure
All the variation is due to that R group – is R on the periodic table?

4. Peptide to Di peptide to polypeptide
Simple – forming the peptide bond
It is a condensation reaction – can you show me how two Gylcine molecules could bond?
No peaking
This is Glycine
Now try the questions on page 62

5. Protein Structure
Primary – the polypeptide chain – can you explain how this is made – on whiteboards
Secondary – Alpha Helix or Beta Pleated sheet – structure is maintained by interactions between CO and NH groups
Which if the secondary is made depends on the R groups so the primary structure – way to complicated to do here

7. Tertiary Structure Made possible due to Ionic bonds Disulphide Bridges
Hydrophobic Hydrophilic interactions
Hydrogen bonds

8. All the different groups of amino acid lead to interactions
Ionic – simple positive to negative R groups
Di-Sulfide bridges – between sulfur atoms
Hydrophobic and Hydrophilic regions – hydrophobic groups stick together (usually in the centre of globular proteins and the hydrophilic regions get pushed to the outside
Hydrogen bonds – Slight negative and positive charged groups attract (weak bonds)

9. Some questions What bonds hold together the primary structure?
What defines the primary structure?
What is the reaction that makes a peptide bond called?
How many amino acids are coded for in your body?
What does aromatic mean in biochemistry?
What is the basic structural formula of an amino acid?
What is the basic molecular formula of an amino acid?

10. Quaternary When more than one protein chain works with another one
Examples
Haemoglobin – four chains

11. Globular and Fibrous Globular are soluble
Have a tertiary structure that readily impacts function
The chains are folded into a spherical shape
Common functions – enzymes, hormones, transport, immunity

12. Hormone Insulin Two chains an A and B chain
All stuck together by Disufide bonds

13. More on Haemoglobin Special bits to consider here
First it is a conjugated protein
This means it has a non protein group stuck on
This is called a prosthetic group in this case Iron containing Haem Group
So simply Haemoglobin is the globular haem containing protein

14. Enzymes Loads of examples
Two are amylase – to break down starch in your digestive system it is made from one polypeptide chain with both alpha and beta sections
RuBisCo – possibly the most important enzyme in the world, and is massive, contains 8 small and 8 large subunits arranged as dimers (in 2). And as if befitting it’s important it is the most abundant protein on earth

15. Structural Proteins These do not dissolve (pretty handy)
Tough and may be supple and stretchy
Made of lots of parallel chains in long fibres or sheets
Examples – Collagen, Myosin, Actin, keratin, elastin

16. Collagen
Made of three helical polypeptides wound round each other like a rope
Every third Amino Acid is a glycine which increases Hydrogen bonding this secures the strands tertiary structure
It is found in all connective tissue on your body, the mineral content changes it’s behaviour – e.g more minerals = bone