1. Warm up What is the difference between micro and macro?
How is organic chemistry defined?
Carbon based compounds

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 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

5. Dehydration Synthesis (Condensation Reaction)
Hydrolysis
Make polymers
Breakdown polymers
Monomers  Polymers
Polymers  Monomers
A + B  AB
AB  A + B
Condensation (DEHYDRATION) reactions: 2 molecules are covalently bonded to each other through loss of a water molecule.
When a polymer is forming, each monomer contributes part of the water like a hydroxyl group or hydrogen.
This reaction is repeated as monomers are added to the chain one by one.
Cell uses energy to carry out this process and only occurs with the help of enzymes.
Hydrolysis: BREAKING DOWN monomers.
Break with water
Bonds are broken by adding water molecules
Hydrogen from water bonds to one monomer and the hydroxyl group to the other,
in our body this happens in digestion, food is in the form of polymers and too big to enter the cells.
enzymes attack polymer, speeding up hydrolysis
+ H2O +
+ H2O +

7. 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)
Monosaccharides- CH2O fomula glucose is the most common. Has carbonyl group, multi hydroxyl groups
Depending on the location of the hydroxyl group they are either aldose- aldehyde sugar or ketose- keytone sugar.
glucose- aldose, fructose –ketose (isomer of glucose)
Another way to classify sugars is based on the size of the carbon skeleton, their spatial arrangement
Usually drawn as chains but in aqueous solutions form rings.
Disaccharide- 2 monosaccharide joined by glycosidic linkage-covalent bond between monosaccharide by dehydration reaction.
example: maltose, lactose
Polysaccharides- macromolecule made of a few 100 monosaccharides
store material
structural- building material that protect the cell or whole organism
Differ in position & orientation of glycosidic linkage

8. The structure and classification of some monosaccharides
Location of carbonyl group
Length of carbon
Spatial arrangements

9. Linear and ring forms of glucose
Chemical equilibrium between linear and ring structures favors the formation of rings. Carbon 1 bonds to oxygen attached to carbon 5
Linear and ring forms of glucose

10. Carbohydrate synthesis
2 glucose bonding by creating h2o and forming a glycosidic linkage between carbon 1 and 4
Glycosidic linkage 1 and 2
Carbohydrate synthesis

11. Cellulose vs. Starch Two Forms of Glucose:  glucose &  glucose
Differ in the placement of the hydroxyl group.
Cellulose tough walls that enclose plants cells. Most abundant organic compound on earth beta
Starch made of glucose, stored in chloroplasts (STORED ENERGY) alpha

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

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

14. Structural polysaccharides: cellulose & chitin (exoskeleton)

15. 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
Little or no affinity to water
Not considered a polymer but are large
Assemble from smaller molecules by dehydration
Glycerol= alcohol group with carbon each with a hydroxyl group
Fatty acid= long chain with carboxyl at one end. (HYDROPHOBIC)
Fats separate becuz water molecules H-bonds to one another and exclude fats.
Hydrophilic head
Hydrophobic tail

16. Glycerol and 3 fatty acids through dehydration water molecule removed for each fatty acid joined to gycerol

17. 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

18. The structure of a phospholipid
2 fatty acids attached to glycerol, phosphate attached to the 3rd hydroxyl group of glycerol. Which has a negative charge. Polar molecules can link to phosphate group.
Cell membrane. Phospholipids bilayer
The structure of a phospholipid

19. Hydrophobic/hydrophilic interactions make a phospholipid bilayer

20. Molecule from which most other steroids are synthesized
Molecule from which most other steroids are synthesized. Vary in functional group as seen in the gold
Cholesterol, a steroid

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

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

24. Overview of protein functions

25. Overview of protein functions

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

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

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

31. 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.

32. 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

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

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

35. Chaperonins assist in proper folding of proteins

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

37. change in structure = change in function

38. 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

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

40. 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

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