1. Warm-Up
What are the 4 classes of macromolecules? Give an example of each.
Draw and label the parts of an amino acid.
How are 2 amino acids put together? Name the process and describe what happens.
Draw a tripeptide. (Use Google for help) Label the peptide bonds.

2. Peptide Bonds

3. Warm-Up What are the 4 classes of macromolecules?
Give an example of each type of macromolecule.

4. Ch. 5 Warm-Up Activity
In your family groups, complete #1-5 on Activity 4/5.1: “How can you identify organic macromolecules?”

5. Warm-Up
What are the 4 levels of protein structure? What bonds are formed in each level?
Which protein was involved in the curds & whey lab yesterday?
Explain what happened to the milk to form the curds and whey.

6. The Structure and Function of Large Biological Molecules
Chapter 5
The Structure and Function of Large Biological Molecules

7. You Must Know
The role of dehydration synthesis in the formation of organic compounds and hydrolysis in the digestion of organic compounds.
How to recognize the 4 biologically important organic compounds (carbs, lipids, proteins, nucleic acids) by their structural formulas.
The cellular functions of all four organic compounds.
The 4 structural levels of proteins
How proteins reach their final shape (conformation) and the denaturing impact that heat and pH can have on protein structure

8. ie. amino acid  peptide  polypeptide  protein
Monomers
Polymers
Macromolecules
Small organic
Used for building blocks of polymers
Connects with condensation reaction (dehydration synthesis)
Long molecules of monomers
With many identical or similar blocks linked by covalent bonds
Giant molecules
2 or more polymers bonded together
ie. amino acid  peptide  polypeptide  protein
larger
smaller

9. Dehydration Synthesis (Condensation Reaction)
Hydrolysis
Make polymers
Breakdown polymers
Monomers  Polymers
Polymers  Monomers
A + B  AB
AB  A + B
+ H2O +
+ H2O +

11. Dehydration Synthesis

12. Hydrolysis

13. I. Proteins “Proteios” = first or primary 50% dry weight of cells
Contains: C, H, O, N, S
Myoglobin protein

14. Protein Functions (+ examples)
Enzymes (lactase)
Defense (antibodies)
Storage (milk protein = casein)
Transport (hemoglobin)
Hormones (insulin)
Receptors
Movement (motor proteins)
Structure (keratin)

15. Overview of protein functions

16. Overview of protein functions

17. Four Levels of Protein Structure
Primary
Amino acid (AA) sequence
20 different AA’s
peptide bonds link AA’s

18. Amino Acid “amino” : -NH2 “acid” : -COOH R group = side chains
Properties:
hydrophobic
hydrophilic
ionic (acids & bases)
“amino” : -NH2
“acid” : -COOH

21. Four Levels of Protein Structure (continued)
Secondary
Gains 3-D shape (folds, coils) by H-bonding
Alpha (α) helix, Beta (β) pleated sheet

22. Basic Principles of Protein Folding
Hydrophobic AA buried in interior of protein (hydrophobic interactions)
Hydrophilic AA exposed on surface of protein (hydrogen bonds)
Acidic + Basic AA form salt bridges (ionic bonds).
Cysteines can form disulfide bonds.

23. Four Levels of Protein Structure (continued)
Tertiary
Bonding between side chains (R groups) of amino acids
H bonds, ionic bonds, disulfide bridges, van der Waals interactions

24. Four Levels of Protein Structure (continued)
Quaternary
2+ polypeptides bond together

25. amino acids  polypeptides  protein
Bonding (ionic & H) can create asymmetrical attractions

26. Chaperonins assist in proper folding of proteins

27. Protein structure and function are sensitive to chemical and physical conditions
Unfolds or denatures if pH and temperature are not optimal

28. change in structure = change in function

29. Function: store hereditary info
II. Nucleic Acids
Function: store hereditary info
DNA
RNA
Double-stranded helix
N-bases: A, G, C, Thymine
Stores hereditary info
Longer/larger
Sugar: deoxyribose
Single-stranded
N-bases: A, G, C, Uracil
Carry info from DNA to ribosomes
tRNA, rRNA, mRNA, RNAi
Sugar: ribose

30. Nucleotides: monomer of DNA/RNA
Nucleotide = Sugar + Phosphate + Nitrogen Base

31. Nucleotide phosphate A – T Nitrogen G – C base 5-C sugar Purines
Pyrimidines
Adenine
Guanine
Cytosine
Thymine (DNA)
Uracil (RNA)
Double ring
Single ring
5-C sugar

33. Information flow in a cell: DNA  RNA  protein

34. Differ in position & orientation of glycosidic linkage
III. Carbohydrates
Fuel and building material
Include simple sugars (fructose) and polymers (starch)
Ratio of 1 carbon: 2 hydrogen: 1 oxygen or CH2O
monosaccharide  disaccharide  polysaccharide
Monosaccharides = monomers (eg. glucose, ribose)
Polysaccharides:
Storage (plants-starch, animals-glycogen)
Structure (plant-cellulose, arthropod-chitin)
Differ in position & orientation of glycosidic linkage

35. The structure and classification of some monosaccharides

36. Linear and ring forms of glucose

37. Carbohydrate synthesis

38. Cellulose vs. Starch
Two Forms of Glucose:  glucose &  glucose

39. Cellulose vs. Starch Starch =  glucose monomers
Cellulose =  glucose monomers

40. Storage polysaccharides of plants (starch) and animals (glycogen)

41. Structural polysaccharides: cellulose & chitin (exoskeleton)

42. II. Lipids Fats (triglyceride): store energy
Glycerol + 3 Fatty Acids
saturated, unsaturated, polyunsaturated
Steroids: cholesterol and hormones
Phospholipids: lipid bilayer of cell membrane
hydrophilic head, hydrophobic tails
Hydrophilic head
Hydrophobic tail

44. Have some C=C, result in kinks
Saturated
Unsaturated
Polyunsaturated
“saturated” with H
Have some C=C, result in kinks
In animals
In plants
Solid at room temp.
Liquid at room temp.
Eg. butter, lard
Eg. corn oil, olive oil

45. Cholesterol, a steroid

46. The structure of a phospholipid

47. Hydrophobic/hydrophilic interactions make a phospholipid bilayer