1. Chapter 4 and 5: The Amazing Carbon Atom and Function of Macromolecules Estimated time: 5 days Learning Goals: 1. Understand why carbon is the basis of living things 2. Organic Chemistry is carbon based chemistry 3. Recognize the functional groups 4. Understand the basics of macromolecule chemistry 1. Carbohydrates 2. Proteins 3. Nucleic Acid 4. Lipids

2. Why Carbon? -Organic Chemistry is the study of carbon based compounds -At some point in Earth’s history organic compounds were created (Miller Experiment) -Hydrocarbons contain only hydrogen and carbon (Fatty acid chains (non polar) Carbon Anatomy -Four valence electrons - Can bond with four other atoms -Can create single, double, and triple bonds (Rings and Resonance)

3. What are Isomers -Carbon has the ability to be the backbone of isomers due to it’s four potential bonds. -Isomers have the same molecular formula but different shapes Structural differ in covalent arrangement of atoms Geometric differ in spacial arrangement -Across double bonds -Trans and Cis Enatomers are mirror images of each other **Look at page 63 for other samples

4. Functional Groups: There are seven major groups that have specific chemical properties 1. Hydroxyl 2. Carbonyl 3. Carbonxyl 4. Amino 5. Sulfhydryl 6. Phosphate 7. Methyl ** You will need to make a foldable with all the functional groups on it. P. 64-65 will help.

5. Macromolecules…. What? - “Macromolecules are the molecules of life” -”Macro cause their big” -Types: -Proteins -Lipids -DNA -Carbohydrates

6. Macromolecule polymer chemistry - Polymers: long chains of monomers - Monomers: Similar units (building blocks) Carbohydrates Monomers = various sugars Protein Monomers = Amino Acids Nucleic Acid Monomers = Nucleotides **Lipids don’t consist of polymers. Hydrolysis = breaks a monomer off the polymer Dehydration = adds monomers to a polymer

7. Carbohydrates -Monosaccarides = one sugar molecule (Follow (CH 2 O) n formula) -Open chain or ring forms www.stolaf.edu/people/.../biological%20anamations.html - Classified by - Classified by: 1. Number of Carbons 2. Aldoses or Ketoses 3. Chiral Carbons

8. Carbohydrates - Polysaccharides = Polymers made up of monosaccarides (different monomers make up different polymers - 1-4 glycosidic bond = Bonds between monosaccharides are between the 1carbon and the four carbon

9. Carbohydrates: Energy Storage - Glycogen – Branched Glucose polymer -Stores glucose in animals -Hydrolysis releases glucose for metabolism - Starch – Branched and Unbranched plant glucose polymers. -Stores glucose in plants -hydrolysis releases glucose for metabolism -Animals can hydrolyze starch Carbohydrates: Structure Cellulose – Long linear chains - Can hydrogen bond with parallel chains Starch vs Cellulose -Structural difference in Glucose (Alpha or Beta) - Starch can be digested by humans -Cellulose can’t be digested by humans http://pslc.ws/macrog/kidsmac/starlose.htm

10. Lipids are … -Non polar -Not considered polymers -Mostly hydrocarbon chains - Fats are considered lipids -Three fatty acids connected to a glycerol molecule -Energy Storage (adipose cells) 1 g has twice as much storage as 1 g of starch -Saturated (solid) vs unsaturated (liquids) contain double bonds p. 75 -Fat is an adaptation - Phospholipids contain a polar (hydrophilic) head and two hydrocarbon, non polar (hydrophobic) tails -Form the lipid bilayers of cells and organelles -Cells wouldn’t exist without phospholipids Steriods - lipids characterized by four carbon rings fused together -Cholesterol found in cell membranes -Hormones like testosterone and estrogen

11. Protein Function -50% of dry mass of most cells is proteins -Extremely large molecules -Act as enzymes p. 78 -Enzymes are biological catalysts that speed up chemical reactions This 3-D model shows the enzyme integrase which is responsible for inserting HIV into the DNA of humans http://www.cbc.ca/technology/story/2010/02/01/tech-aids-enzyme-structure.html Active Site

12. Protein Composition -Proteins are polypeptide chains -Made up of monomers called amino acids -Amino acids have various properties -Properties determine folding and overall protein function -Proteins are made in the ribosomes and coded for in DNA

13. Protein Structure Primary Structure -Amino Acid Sequence -Can be thought of as a book Secondary Structure is dictated by amino acid sequence (polar amino acids) that form hydrogen bonds Alpha Helix and Beta pleated sheets Tertiary Structure Uses all the molecular attractions to hold the protein together. Quaternary Structure -Bonding of more then one protein sequence. -Can use units like iron to hold together.

14. Sickle Cell Example -Read p. 84. -Example of how a single error in the primary structure can effect the rest of the structures

15. Protein Craziness -Proteins will fold the correct way provided a proper environment -Temperature and pH have an affect on pH. -Protein Chaperones can create a proper environment for other protein folding -Alzheimer’s and Parkinson’s are associated with misfolded proteins

16. Nucleic Acid Function 1. Store and transfer genetic information 2. Can exist as DNA (double stranded) 3. Can exist as various types of RNA (single stranded) mRNA, tRNA, rRNA

17. Nucleic Acid Composition -Monomers are nucleotides made up of one sugar, one phosphate group and one nitrogenous base -Bases differ in structure -Sugars differ depending on if RNA or DNA

18. Nucleic Acid Structure -Double Helix Structure -Anti-parallel (5’ – 3’) -Bases are bound by hydrogen bonds -Sugars and phosphate groups alternate on the backbone.