1. I. The Structure and Function of Macromolecules

2. A. Macromolecule- Large molecules, some with molecular weights exceeding 100,000 Daltons
Macromolecules are composed of polymers. Chains of similar subunits
Monomers- individual subunits that make up polymers
Polymers and molecular Diversity
All macromolecules are composed of of the same monomers
All proteins in all organisms are made of the same 20 amino acids. Just as 26 letters make all words

3. 4. Making a Breaking Polymers
Condensation Reaction- usually occurs between –OH groups of two monomers. H2O is removed linking the monomers with an oxygen bridge
Hydrolysis- breaking apart polymers at their oxygen bridge by adding H2O which results in two monomers

4. B. Carbohydrates- sugars and starches that serve as important sources of fuel and structural components

5. Carbohydrates
Monosaccharides- single sugars with 3-6 carbons. (Glucose, Fructose, Galactose)
Disaccharides- two monosaccharides joined in a condensation reaction
Polysaccharides- many single sugars joined together

6. Types of Polysaccharides
Starch- storage form of carbohydrate in plants. (Spiraling 1-4α glycosidic bonds)
Glycogen- Storage form of carbohydrates in animals. (Spiraling, highly branched, 1-4α glycosidic bonds)
Cellulose- Structural polysaccharide in plants. (Straight polysaccharide with 1-4β glycosidic bonds)

7. 4. Modified Carbohydrates
A) Chitin- main component of the exoskeletons of arthropods. Contains a monosaccharide derivative glucosamine

8. Lipids
Animal Fat
Plant Oils
Waxes

9. C. Lipids- molecules used to store energy in organisms as well as structural materials. Made of C, H, O. Less oxygen than in carbohydrates. Twice the amount of energy. Soluble in non-polar solvents

10. 1. Neutral Fats- 1 glycerol with fatty acid chains

11. Types of Lipids
a) Saturated fat- Solid at room temperature. Many hydrogen. No double bonds between carbons. Animal fats. Cause arteriosclerosis.

12. b) Unsaturated and Polyunsaturated Fat- Oils
b) Unsaturated and Polyunsaturated Fat- Oils. Liquid at room temperature. Double bond between some of the carbons. 2 essential fats are oleic and linoleic acid. These cannot be synthesize by the body but must be in the diet

13. 2. Phospholipid- important constituents of the cell membrane made of a glycerol and 1-2 fatty acid chain with the glycerol bonded to a phosphate group. Contains a hydrophilic and hydrophobic end

14. Other Lipids
3.Carotenoids- red and yellow plant pigments that play a role in photosynthesis
splitting the orange plant pigment carotene yeilds a retinol molecule
Retinol molecules play an important role as photoreceptors in eyes
4. Steroids- class of compounds with four interlocking rings to form many biologically important molecules (Cholesterol, bile salts, hormones etc….)

15. D. Proteins- all enzymes, some hormones and many structural components of the cell are proteins.

16. 1. Subunit Structure (Protein monomer = Amino Acid)
a) Amino acids are composed of an amino group (-NH2) and an acidic carboxyl group but different r groups
R group
Amino group
Carboxyl group
b) The “R” group determines the identity of the amino acid

17. Amino Acids with Hydrophobic Side Groups
Note the methyl groups at the bottom of the chains

18. Amino Acids with Hydrophilic Side Groups
Note the charged or polar groups at the bottom of the chains

19. And Some Amino Acids are in Between
Hydrophobic and Hydrophilic regions influence protein shape.

20. C) Amino acids can serve as acids or bases and are therefore considered buffers
D) Amino acids are linked by a condensation reaction and form peptide bonds
E) When many amino acids are joined, a polypeptide is formed

21. 2. Levels of Protein Structure
Primary- Linear sequence of amino acids joined by peptide bonds in a condensation reaction
Secondary- coiling and pleating of amino acid chains (α helixes or β pleats) stabilized by hydrogen bonds
Tertiary- overall shape caused by the folding or twisting of the secondary structure
Quaternary Intertwining of multiple polypeptides to produce a highly specific 3D shape

22. 3. Importance of Proteins
a) Proteins are the most abundant molecule in living cells. Functionally diverse, They control all life functions
Class Function Example
A) Enzymes. Control Chemical Reactions. Maltase
B) Structure. Building material of cells. Collegen
C) Contractile. Movement Actin and myosin
D) Hormones. Regulatory chemicals Insulin
E) Transport. Ship important substances hemoglobin
F) Defense Fight Disease antibodies
c) Proteins are sensitive and may denature (change shape) and become non functional. Heat, pH and metals all can cause denaturation

23. E. Nucleic Acids- large complex molecules formed of smaller smaller units called nucleotides
1. Nucleic Acid structure (monomer = nucleotide)
Nucleotide consists of a sugar a phosphate group and a nitrogen base
Sugars:
Ribose in RNA
Deoxyribose in DNA
c) Bases:
1) Purines (2 rings) Adenine and Guanine
2) Pyrimidines (1 ring) cytosine and Thymine

24. Nucleic Acids
DNA structure is a double helix with the base pairing of Thymine & Adenine and Cytosine & Guanine.
RNA structure is a single spiral with Uracil replacing thymine.

25. 4. Nucleic Acid Function
DNA carries the genetic code. The information for constructing proteins
RNA Carries the genetic code to the ribosome.
Adenosine Triphosphate (ATP) supplies energy to the cell
Other Nucleotides and dinucleotides are electron transport molecules and energy carriers
GTP, UTP, CTP
dGTP, dATP, dCTP, dTTP
AMP, NAD+, NADP, FAD