1. Carbon & Macromolecules
Chapters 4 & 5

2. I. Building Blocks Carbon!!!
1. Uniquely suited to being the foundation of biological molecules – 4 valence electrons
2. Forms four covalent bonds to fill its outer electron shell
a. Remember – covalent bonds are strong and stable
b. Can be a combination of single, double, and triple bonds
c. Allows it form large molecules that can be chains, rings, or branched

3. 1. Molecules with the same formula but different atom arrangements
B. Isomers
1. Molecules with the same formula but different atom arrangements
2. Results in them having different biological activities
3. Ex. Glucose and Fructose – C6H12O6

4. C. Functional Groups
1. Small groups of atoms with diverse properties that attach to a carbon skeleton
2. Properties of a macromolecule arise from the properties of the functional groups it contains

5. II. Organic Molecules
A. Carbon-based molecules that are the basis of all biological organisms
1. Big exception = carbon dioxide – not organic
2. Fall into one of four categories
a. Carbohydrates
b. Lipids
c. Proteins
d. Nucleic Acids
3. Also called macromolecules, biomolecules, polymers
*Polymers are large molecules made of repeating subunits*

6. Macromolecule Elements Subcomponents/ monomers Function
Carbohydrates
(aka polysaccharides)
C, H, O
Monosaccharides, disaccharides (aka sugars)
Energy source, short-term energy storage
Lipids
Usually glycerol combined with fatty acids
Long-term energy storage, cell membranes, hormones
Proteins
(aka polypeptides)
C, H, O, N
Amino Acids
Regulate reactions, transport molecules, membrane channels and pumps, chemical messengers, fight disease
Nucleic Acids
C, H, O, N, P
Nucleotides
Store and transmit genetic information, code for and help build proteins

7. B. Carbohydrates 1. Ratio of 1 carbon : 2 hydrogen : 1 oxygen
2. Monomers are monosaccharides (aka simple sugars) such as glucose, fructose, ribose
3. Polysaccharides (aka complex carbs) are polymers of monosacchraides such as starch, cellulose, and glycogen
4. Functions include energy source, short- tem energy storage, and structural support

8. 5. Examples
Component of plant cell walls Energy storage in plants Energy storage in animals Component of arthropod exoskeletons

9. a. Can be linear or branched

10. C. Lipids 1. Large, hydrophobic molecules – fats, oils, waxes
2. Not considered polymers – no repeating monomers
3. Triglycerides (fats) – composed of a glycerol backbone and 3 fatty acid molecules (hydrocarbon chains – non-polar)
4. Functions – Long-term energy storage,
protection and insulation, component
of cell membranes, steroids such as
cholesterol, estrogen, and testosterone

11. 5. Saturated vs. Unsaturated Fatty acids
-All single bonds between the carbons of the hydrocarbon chain (saturated with hydrogen)
-Pack together tightly
-Usually solid at room temperature
-Linked to cardiovascular disease
-Ex. butter, bacon grease, Crisco (animal fats)
Unsaturated Fatty Acids
Contain one (monounsaturated) or more (polyunsaturated) double bonds between the carbons in the hydrocarbon chain
Causes “kinking” of the chain
Can’t pack as tightly together
Usually liquid at room temperature
Ex. Vegetable oil, olive oil (plant fats)

12. 1. Polymers of amino acids
Proteins
1. Polymers of amino acids
Prope
*The properties of the R groups and their interactions determine the structure and function of the protein

13. 2. Have 4 levels of structure

14. a. Primary Structure - the order in which amino acids are strung together
This order is coded for by genes

15. b. Secondary Structure - carboxyl groups and amine groups of the non-adjacent amino acids interact and form hydrogen bonds with each other, resulting in either alpha helix or beta pleated sheet
***Both types of secondary structure are generally found in all proteins

16. c. Tertiary Structure - 3-D folding created by bonds forming between the R groups of the various amino acids (hydrogen bonds, ionic bonds, disulfide bridges, and non-polar interactions are the most common)
Can result in globular or fibrous structures

17. d. Quaternary Structure - Some (not all
d. Quaternary Structure - Some (not all!) proteins are composed of multiple polypeptides or are associated with prosthetic groups (non- polypeptide molecules like iron, lipids, sugars, vitamins)

18. 3. The function of a protein is entirely dependent on its shape!
a. Quaternary structure is dependent on tertiary structure which is dependent on secondary structure which is dependent on primary structure – if you change the primary structure, you change the protein’s secondary, tertiary, and quaternary structure, making it unable to perform its function

19. b. Proteins have a wide variety of functions
Regulate reactions (enzymes)
Transport molecules in the blood (hemoglobin)
Chemical messengers (hormones, neurotransmitters)
Channels and pumps in the cell membrane
Cell-to-cell communication (transmit/receive signals)
Fight disease (antibodies)
Provide structure and support
Contract to cause movement

20. E. Nucleic Acids
1. Monomers are nucleotides
2. Polymers – DNA and RNA

21. III. Metabolism
Metabolism is the total of all the chemical reactions in an organism and mostly consists of building (anabolism) and breaking down (catabolism) macromolecules
Organisms must exchange matter with the environment and then assimilate that matter into molecules the organism needs to function

22. Anabolism – building macromolecules
1. Put together components (generally monomers) to make larger molecules (generally polymers)
2. Use condensation/dehydration reactions – remove a molecule of water to bond together monomers

23. Catabolism – breaking down molecules
1. Breaking a polymer down into monomers
2. Use hydrolysis reactions – put water in to break monomers apart

24. E. Types of covalent bonds between monomers
Carbs – glycosidic bonds
Lipids – ester bonds

25. Proteins – peptide bonds
Nucleic acids – phosphodiester bonds