1. Chapter 5 Protein Pipe cleaner Supplies
1 Pipe cleaner per student
30-50 pony beads per student
Bowl to hold in
Few larger sized beads
Yellow beads and yellow paper clips for S bonds
Needle and thread for H bonding.

2. Chapter 5
Group your questions about Lipids and Proteins. Everyone must post at least 1!

3. The Structure and Function of Large Biological Molecules
Chapter 5
The Structure and Function of Large Biological Molecules
4.a.1Interactions within biological systems lead to complex properties: The subcomponents of biological molecules and their sequences determine the properties of that molecule.
4.c.1 Naturally occurring diversity among and between components within biological systems affects interactions with the environment: Variation in molecular units provides cells with a wider range of functions

4. Remember 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
Print and distribute slide 4&5

5. 4 Classes of large biological molecules
Carbohydrates
Lipids
Proteins
Nucleic acids

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

7. Protein Functions (+ examples)
Enzymes (lactase)
Defense (antibodies)
Storage (milk protein = casein)
Transport (hemoglobin)
Hormones (insulin)
Receptors
Movement (motor proteins)
Structure (keratin)
Cellular Communication
Animation of many types of Proteins
Type, function, example listed on table 5.1
Watch the animation 1st then talk about each
Animations are listed in Campbells ppt but I can not find them

8. Did you name all the peices
Enzymes are very important concept. Covered more later in ch8. Has an animation I cant find.
Enzymes are a type of protein that acts as a catlyst to speed up chemical reactions repeatedly without being used up or changed.

9. Overview of protein functions

10. Overview of protein functions

11. Four Levels of Protein Structure
Primary
Amino acid (AA) =organic
molecule: carboxyl & amine
and different R groups
20 different AA’s
Polypeptide= polymers of
some variation of the 20AAs
26letters=millions words
sequence!
peptide bonds link AA’s

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

14. 1o Sequence Pipe Cleaner Proteins
Beads are the AA
String them on the pipe cleaner
Red are hydrophobic
which AAs?
Blue are hydrophilic
which Aas?
Yellow is thiol containing.
How will you string them with this in mind?
When you string them what bonds are you making between the Aas?
What are the reactions called
Journal about each of these. Draw your pipe cleaner.
Figure 5.16 p79
Prize to student that thinks through it well enough to not have to restring often.
Give students 1 pipe cleaner, beads, yellow paper clip, bowl, few instructions so they have to do it on their own.

15. Four Levels of Protein Structure (continued)
Secondary
Gains 3-D shape (folds, coils) by H-bonding
Alpha (α) helix, Beta (β) pleated sheet
How will you model the alpha and beta shapes?
How will you maintain the shape?
What colors do you have to pay attention to and why?
What does alpha mean= spiral shape caused by h bonding when the OH groups are all on the same side (Show by twisting around pencil and needle and thread to hold together)
What does beta mean=folded shape caused by H bonding when the OH groups are on opposite sides. (Show by folding up and down accordion style.) hold together with needle and thread
The nonpolar will not allow the Hbonding so cant sew between red beads

16. 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
Clearly illustrate the Disulfide bonds, check with your teacher. You decide and justify how you want to list the rest.
Draw and journal
Great image. Know every aspect of this.
Use the yellow paper clip to hold the yellow cystine groups together in a SS bridge,
Let students show how to illustrate all bonds

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

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

19. Chaperonins assist in proper folding of proteins

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

21. change in structure = change in function

22. 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

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

24. 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

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

27. 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

28. The structure and classification of some monosaccharides

29. Linear and ring forms of glucose

30. Carbohydrate synthesis

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

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

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

34. Structural polysaccharides: cellulose & chitin (exoskeleton)

35. 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

37. 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

38. Cholesterol, a steroid

39. The structure of a phospholipid

40. Hydrophobic/hydrophilic interactions make a phospholipid bilayer