1. Review  Draw each chemical group without looking: Hydroxyl,  Carbonyl, Carboxyl, Amino, Sulfhydryl, Phosphate and Methyl.  Once you have tried without looking, you may check your work by looking in the book or in your notes

3. Be able to…  Name all 4 macromolecules of life and their main functions  Name examples of where they are found in the cell

6. Macromolecules – huge molecules in living organisms that are essential to life  Polymer – long molecules consisting of many similar building blocks  Monomer – the small building blocks

7.  Get in a line and do the cho cho train. Put your hand on the shoulder of the person in front of you.

8. Carbohydrates – sugars and polymers of sugars  Monosaccharides – one sugar *Be able to recognize the difference between glucose and fructose in their ring structure Glucose

9. Carbohydrates  Disaccharides – two sugars Glucose + Fructose = Sucrose (table sugar) Glucose + Glucose = Maltose Galactose + Glucose = Lactose

10. Carbohydrates  Polysaccharides – many sugars Starch – Helix shaped (storage) Cellulose – Long strands “cable like” shape(structural) Glucose polymers Plant starchesGlycogen - Animal starch Amylopectin (Branched) Amylose (unbranched)

12. Lipids – mix poorly with water  Types Fats – stores energy Phospholipids – the membranes around your cells Steroids – such as hormones Fats Phospholipids Steroids

13. Fats  Unsaturated – a double bond (makes a kink in the chain)  Saturated – no double bonds ( all straight chains)

14. Lipids - Phospholipids  Hydrophillic head – can bond to water  Hydrophobic tail – does not bond to water

15. Proteins  Structure Primary Secondary Tertiary Quaternary

16. Proteins – Primary structure  The small subunits make up a polypeptide chain just as letters make up words  20 different amino acids, so if it was 127 amino acids long then there would be 20 127th different ways of making a polypeptide chain

17. Proteins – Secondary structure  α Helix and β pleated sheet They bond because of the hydrogen bonds in the backbone (the oxygen and hydrogen)

18. Proteins – Tertiary structure  All of the α Helix and β pleated sheets fold in on each other The chemical bonding is due to the R-groups (side chains). Ex. Hydrophobic (non polar side chains accumulate on the inside of a protein if there is water outside the protein) or Ionic bonds resulting from side chains

19. Proteins – Quaternary structure  More than one polypeptide chain “globs” together

20. Antibody protein Protein from flu virus Structure and function: Proteins have a specific shape that helps bind specific molecules

21. Nucleic acids – DNA and RNA  Carries information to synthesize polypeptides DNA RNA Proteins

22. Structure of Nucleic acids  The monomer (nucleotide) is made of a phosphate group, a sugar (pentose) and a nitrogenous base