1. Problem of the Day: What type bonds are found at: A? Polar Covalent B? Hydrogen How does bond A cause bond B? It pulls electrons unequally and results in a charge on the end of the molecule. Opposite charges attract.

2. Mr. Anderson Biomolecules

3. Organic Chemistry You Must Know: The properties of carbon that make it so important for life How structure determines function in biological molecules The role of dehydration and hydrolysis reactions How to recognize the four types of biologically important molecules Cellular functions of these molecules How proteins reach their final shape (4 levels/interactions)

4. Essential Knowledge 4.A.1 The subcomponents of biological molecules and their sequence determine the properties of that molecule. Structure and function of polymers are derived from the way their monomers are assembled. (proteins have a specific order of amino acids) Directionality influences structure and functions of the polymer (ex. DNA is read in a certain order by mRNA to code for a gene). Structure and directionality determine the shape of the molecule. Shape directly influences function.

5. Carbon-most versatile building block of molecules. Why? 4 valence electrons Can form 4 single covalent bonds Capable of forming double and triple covalent bonds Can combine with atoms of many different elements Can form chains, rings and branching structures

6. Isomers Isomers (same molecular formula, but different structure & properties) –structural~ differing covalent bonding arrangement –geometric~ differing spatial arrangement –enantiomers~ mirror images pharmacological industry (thalidomide)

7. The Pharmacological Importance of Enantiomers

8. Functional Groups (Polyatomic Ions) Small characteristic groups of atoms that are bonded to the carbon skeleton Have specific chemical and physical properties Consistent from one organic molecule to another Determine the unique chemical properties of the organic molecule in which they are found They are the parts of molecules involved in chemical reactions DNA Methylation and expression of genes

9. Functional Groups Attached to the carbon skeleton of a biological molecule Determine the behavior of the molecule methyl

10. Just how important are functional groups? Closely examine the two organic molecules in the picture. What differences are there? How significant are the consequences?

12. Structure and Function of Macromolecules 3 themes are emphasized Hierarchy of structural levels Emergent properties Form fits function

13. Polymers and Reactions Large molecules of many repeating subunits called monomers Condensation reaction or dehydration reaction; monomers are joined by removing a water molecule=polymers Hydrolysis-addition of water and breaking of polymers into smaller units

15. Bond Formation in Macromolecules

16. Classes of Polymers Classes of Polymers Carbohydrates Lipids Proteins Nucleic Acids

17. Carbohydrates Ratio of 1 carbon: 2 hydrogen: 1 oxygen Monomers-monosaccharides; simple sugars like glucose, fructose, galactose Polymers- polysaccarides; Functions: –Energy storage (starch and glycogen) –Structural support (cellulose and chitin)

18. Lipids All hydrophobic Not polymers Fats are a glycerol molecule and 3 fatty acid chains saturated vs. unsaturated Phospholipids-glycerol and 2 fatty acids chains Examples include cholesterol, waxes, butter, vegetable oil Ratio of CHO is 1:2:very few Functions: –Energy storage –Protection of vital organs –Phospholipids- arranged in a bilayer with hydrophilic heads pointing in/out of cell and hydrophobic tails inside the bilayer

19. Lipids

20. Lipids Saturated No double bonds between carbons Tend to pack solidly at room temperature Linked to cardiovascular disease Commonly produced by animals Butter and lard Unsaturated Some carbons that are double bonded-this results in kinks Tend to be liquid at room temperature Commonly produced by plants Corn oil and olive oil

21. Proteins Monomers-amino acids; there are 20 amino acids –Amino acids consist of a central carbon atom bonded to a carboxyl group, and amino group and an R group Polymers are polypeptides Peptide bonds Examples include hemoglobin, peroxidase, pepsin No reliable CHO ratio Always have N and frequently S 4 levels of structure-see next slide Protein shape is crucial to protein function Proteins are denatured (lose shape) by changes in temperature and pH Functions –Enzymes, structure, movement

22. Proteins-4 levels of structure

24. Denaturation Denaturation is the loss of the natural configuration or shape of the protein. Denatured proteins are biologically inactive. Agents that can cause denaturation are changes to pH, salt concentration, temperature or chemical agents such as chloroform and ether.

25. Nucleic Acids Monomers are nucleotides Polymers are nucleic acids DNA and RNA are the only nucleic acids Used for transmission of information (heredity, code for amino acids) No reliable CHO ratio Always contain P, N, usually no S RNA –Single stranded –AUCG –Ribose sugar DNA –Double stranded –ATCG –Hydrogen bonds between the 2 strands –Deoxyribose sugar

26. Nucleic Acids

27. Inheritance based on DNA replication Double helix (Watson & Crick - 1953) H bonds~ between paired bases van der Waals~ between stacked bases A to T; C to G pairing –A to T has 2 H bonds –C to G has 3 H bonds Complementary

28. Other Hybrid molecules Lipoproteins, glycolipids, and glycoproteins Form ECM (extra cellular matrix)

29. Something to wrap your head around: New DNA nucleotides are added at the 3’ end of each side of the DNA molecule. If you look at figure 16.14 on p. 315, you can see this. This means that DNA synthesis goes in the DIRECTION of 5’ to 3’. This also applies to the reading of the DNA molecule by mRNA (transcription)

30. Identify that molecule!