1. Ch. 5 Warm-Up Activity
What are the 4 biologically important organic compounds, their building blocks and an example of each?
What is the difference between dehydration synthesis and hydrolysis? When are each used?
What are the 4 structural levels of a protein and what bonds are involved in each?
What does it mean when a protein has been denatured? What are some possible causes for this to happen?

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

3. 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

4. ie. amino acid  peptide  polypeptide  protein
Monomers
Polymers
Macromolecules
Small organic
Used for building blocks of polymers
Connects with condensation reaction (dehydration reaction)
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

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

7. Differ in position & orientation of glycosidic linkage
I. 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 (ie. glucose, ribose)
Polysaccharides:
Storage (plants-starch, animals-glycogen)
Structure (plant-cellulose, arthropod-chitin)
Differ in position & orientation of glycosidic linkage

8. The structure and classification of some monosaccharides

9. Linear and ring forms of glucose

10. Examples of disaccharide synthesis

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

12. Structural polysaccharides: cellulose & chitin (exoskeleton)

13. II. Lipids
Fats (triglyceride): store large amounts of energy (2x carbohydrates), cushions organs and insulates body
Glycerol + 3 Fatty Acids
saturated, unsaturated, polyunsaturated
Steroids: cholesterol and hormones
Phospholipids: cell membrane
hydrophilic head, hydrophobic tails
creates bilayer to form cell membrane
Hydrophilic head
Hydrophobic tail

14. Ester linkage:
between OH
& COOH
Long HC chain:
-Polar or
non-polar?
-Hydrophilic or
hydrophobic?

15. 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

16. Steroids include cholesterol (shown above) which is the building block for steroid hormones and component of cell membranes

17. The structure of a phospholipid

18. Hydrophobic/hydrophilic interactions make a phospholipid bilayer

19. Overview of protein functions

20. Overview of protein functions

21. Proteins: polymers made of amino acid monomers

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

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

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

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

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

27. Chaperonins assist in proper folding of proteins

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

29. change in structure = change in function

30. Function: carry hereditary info
IV. Nucleic Acids
Function: carry 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

31. Nucleotides: monomer of DNA/RNA
3 parts:
-nitrogen base
-pentose sugar
-ribose
-deoxyribose
-P04 group

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

34. Building the polymer

35. Nucleic polymer Backbone Sugar to PO4 bond Phosphodiester bond
new base added to sugar of previous base
Polymer grow in one direction
N bases hang off the sugar-phosphate
backbone

36. Pairing of nucleotides
Nucleotides bond between DNA strands
H bonds
Purine :: Pyrimidine
A :: T
2 H bonds
G :: C
3 H bonds

37. DNA  RNA  protein: a diagrammatic overview of information flow in a cell.