1. SCI.9-12.B [Indicator] - Summarize how the structures of organic molecules (including proteins, carbohydrates, and fats) are related to their relative caloric values.
SCI.9-12.B [Indicator] - Summarize the functions of proteins, carbohydrates, and fats in the human body.

2. *Organic Compounds Compounds that contain CARBON are called organic.
Macromolecules are large organic molecules.

3. *Carbon (C) Carbon has 4 electrons in outer shell.
Usually bonds with C, H, O or N.
Example: CH4(methane)

4. *Macromolecules Large organic molecules. Also called POLYMERS.
Made up of smaller “building blocks” called MONOMERS.
Examples:
1. Carbohydrates
2. Lipids
3. Proteins
4. Nucleic acids (DNA and RNA)

5. *Question: How Are Macromolecules Formed?

6. *Answer: Dehydration Synthesis
Also called “condensation reaction”
Forms polymers by combining monomers by “removing water”. HO H
H2O HO H
copyright cmassengale

7. *Question: How are Macromolecules separated or digested?

8. *Answer: Hydrolysis
Separates monomers by “adding water” HO H
H2O HO H

9. SCI.9-12.B [Indicator] - Summarize how the structures of organic molecules (including proteins, carbohydrates, and fats) are related to their relative caloric values.
SCI.9-12.B [Indicator] - Summarize the functions of proteins, carbohydrates, and fats in the human body.

10. Carbohydrates

12. *I. Carbohydrates Small sugar molecules to large sugar molecules.
Examples:
A. monosaccharide
B. disaccharide
C. polysaccharide

13. *Carbohydrates Monosaccharide: one sugar unit
Examples: *glucose (C6H12O6)
deoxyribose
ribose
Fructose
Galactose
glucose

14. *Carbohydrates Disaccharide: two sugar unit Examples:
*Sucrose (glucose+fructose) table sugar
*Lactose (glucose+galactose)
Maltose (glucose+glucose)
glucose

15. *Carbohydrates Polysaccharide: many sugar units
Examples: starch (bread, potatoes)
glycogen (beef muscle)
cellulose (lettuce, corn)
glucose
cellulose

17. SCI.9-12.B [Indicator] - Summarize how the structures of organic molecules (including proteins, carbohydrates, and fats) are related to their relative caloric values.
SCI.9-12.B [Indicator] - Summarize the functions of proteins, carbohydrates, and fats in the human body.

18. *II. Proteins
Amino acids are the monomers that make up proteins (20 different kinds of aa) bonded together by peptide bonds (polypeptides). Essential and non-essential
Six functions of proteins:
1. Storage: albumin (egg white)
2. Transport: hemoglobin
3. Regulatory: hormones
4. Movement: muscles
5. Structural: membranes, hair, nails
6. Enzymes: cellular reactions

19. H.B.2A.1 Construct explanations of how the structures of carbohydrates, lipids, proteins, and nucleic acids (including DNA and RNA) are related to their functions in organisms.

20. Amino acids
Are organic molecules possessing both carboxyl and amino groups
Differ in their properties due to differing side chains, called R groups

21. Twenty Amino Acids 20 different amino acids make up proteinsH
H3N+ C
CH3 CH
CH2 NH
H2C
H2N
Nonpolar
Glycine (Gly)
Alanine (Ala)
Valine (Val)
Leucine (Leu)
Isoleucine (Ile)
Methionine (Met)
Phenylalanine (Phe)
Tryptophan (Trp)
Proline (Pro)
H3C
Figure 5.17 S
20 different amino acids make up proteins

22. Polar Electrically chargedOH
CH2 C H
H3N+ O
CH3 CH SH
NH2
Polar
Electrically
charged –O
NH3+
NH2+
NH+ NH
Serine (Ser)
Threonine (Thr)
Cysteine
(Cys)
Tyrosine
(Tyr)
Asparagine
(Asn)
Glutamine
(Gln)
Acidic
Basic
Aspartic acid
(Asp)
Glutamic acid
(Glu)
Lysine (Lys)
Arginine (Arg)
Histidine (His)

23. *Primary Structure
Amino acids bonded together by peptide bonds (straight chains)
aa1
aa2
aa3
aa4
aa5
aa6
Peptide Bonds
Amino Acids (aa)

24. Proteins (Polypeptides)
Four levels of protein structure:
A. Primary Structure
B. Secondary Structure
C. Tertiary Structure
D. Quaternary Structure

25. Secondary Structure
3-dimensional folding arrangement of a primary structure into coils and pleats held together by hydrogen bonds.
Two examples:
Alpha Helix
Beta Pleated Sheet
Hydrogen Bonds

26. Tertiary Structure
Secondary structures bent and folded into a more complex 3-D arrangement of linked polypeptides
Bonds: H-bonds, ionic, disulfide bridges (S-S)
Call a “subunit”.
Alpha Helix
Beta Pleated Sheet

27. Quaternary Structure Composed of 2 or more “subunits”
Globular in shape
Form in Aqueous environments
Example: enzymes (hemoglobin)
subunits

28. SCI.9-12.B [Indicator] - Summarize how the structures of organic molecules (including proteins, carbohydrates, and fats) are related to their relative caloric values.
SCI.9-12.B [Indicator] - Summarize the functions of proteins, carbohydrates, and fats in the human body.

29. *
Proteins must be in a certain shape to function. If you take it out of its shape, you have denatured it and it can not longer work. Heat and pH can denature a protein.
Proteins often change colors when they are denatured. Cooking egg white is an example.

30. Denaturation is when a protein unravels and loses its native conformation (shape)
Renaturation
Denatured protein
Normal protein
Figure 5.22

31. Video on Protein Denaturation

32. *2 types of amino acids
Non-essential amino acids are those your body can make. There are 12.
Essential amino acids are those you must get in your diet because your body cannot make them. There are 8.
If you don’t get the essential aa, you develop kwashiorkor.

33. Review of Protein Structure
+H3N
Amino end
Amino acid
subunits
helix

34. SCI.9-12.B [Indicator] - Summarize how the structures of organic molecules (including proteins, carbohydrates, and fats) are related to their relative caloric values.
SCI.9-12.B [Indicator] - Summarize the functions of proteins, carbohydrates, and fats in the human body.

35. Enzyme reactions
enzyme + substrate
enzyme-substrate complex

36. Enzymes. -- Are defined as a BIOLOGICAL catalyst i. e
*Enzymes -- Are defined as a BIOLOGICAL catalyst i.e. something that speeds up a reaction. Up to 1012 fold
*Usually end in ‘…ase’ and named for what they do or act on (sucrase breaks down sucrose)
Discovered in 1900 in yeasts. Some 40,000 in human cells
*Control almost every metabolic reaction in living organisms
Are globular proteins coiled into a very precise 3-dimentional shape with hydrophilic side chains making them soluble

37. Do not ‘create’ reactions Widely used in industrial cleaning
Possess an active site into which other substrate molecules can bind to form an enzyme-substrate complex
*Once the substrate has been either synthesised or split, enzymes can be re-used.
Do not ‘create’ reactions
Widely used in industrial cleaning
Often require co-factors (co-enzymes) to function – metal ions, or vitamins
SUCROSE IS SUBSTRATE – SUCRASE IS ENZYME
Examples of co-factors and coenzymes. Get those notes from someone.

38. Enzyme reactions
enzyme + substrate
enzyme-substrate complex
E +S ES

39. Enzyme reactions enzyme + substrate enzyme-substrate complex E +S ES
enzyme + product
enzyme-substrate complex ES
E +P

40. How fast an enzyme is working
*Enzyme activity
How fast an enzyme is working
Rate of Reaction
Rate of Reaction = Amount of substrate changed (or amount product formed) in a given period of time.

41. Enzyme activity
Rate of Reaction
Variable you are looking at

42. H.B.2A.2 Plan and conduct investigations to determine how various environmental factors (including temperature and pH) affect enzyme activity and the rate of biochemical reactions.

43. *Enzyme activity
Four Variables

44. *Enzyme activity Temperature pH Enzyme Concentration
Four
Variables
Enzyme Concentration
Substrate Concentration

45. Temperature
Rate of Reaction

46. Temperature
Rate of Reaction 10 20 30 40 50 60

47. Temperature 5- 40oC Increase in Activity 40oC - denatures
Rate of Reaction 10 20 30 40 50 60
<5oC - inactive

48. *Effect of heat on enzyme activty
If you heat the protein above its optimal
temperature, bonds break and the protein loses
it secondary and tertiary structure.
Cooking an egg denatures the proteins and it goes white.
Cooking meat denatures the proteins and it turns brown.

49. Effect of heat on enzyme activty
Denaturing the protein

50. Effect of heat on enzyme activty
Denaturing the protein
ACTIVE SITE CHANGES SHAPE
SO SUBSTRATE NO LONGER FITS

51. pH
Rate of Reaction 1 2 3 4 5 6 7 8 9

52. pH
Narrow pH optima
Rate of Reaction 1 2 3 4 5 6 7 8 9

53. pH
Narrow pH optima
WHY?
Rate of Reaction 1 2 3 4 5 6 7 8 9

54. Effect charged residues at activepH
Narrow pH optima
Disrupt Ionic bonds - Structure
Rate of Reaction
Effect charged residues at active
site 1 2 3 4 5 6 7 8 9

55. SCI.9-12.B [Indicator] - Summarize how the structures of organic molecules (including proteins, carbohydrates, and fats) are related to their relative caloric values.
SCI.9-12.B [Indicator] - Summarize the functions of proteins, carbohydrates, and fats in the human body.

56. *III. Lipids
General term for compounds which are not soluble in water.
Lipids are soluble in hydrophobic solvents, not water.
Remember: “stores the most energy”
Examples: 1. Fats
2. Phospholipids
3. Oils
4. Waxes
5. Steroid hormones
6. Triglycerides

57. *Lipids Six functions of lipids: 1. Long term energy storage
2. Protection against heat loss (insulation)
3. Protection against physical shock
4. Protection against water loss
5. Chemical messengers (hormones)
6. Major component of membranes (phospholipids)

58. *Fatty Acids
There are two kinds of fatty acids you may see these on food labels:
1. Saturated fatty acids: no double bonds (bad)
2. Unsaturated fatty acids: double bonds (good) O
C-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH3 =
saturated O
C-CH2-CH2-CH2-CH
=CH-CH2-CH2-CH2-CH2-CH3 =
unsaturated

59. *Lipids Triglycerides: composed of 1 glycerol and 3 fatty acids. = =H
H-C----O
glycerol O
C-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH3 = O
C-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH2-CH3 =
fatty acids O
C-CH2-CH2-CH2-CH
=CH-CH2-CH2-CH2-CH2-CH3 =

60. *Steroid Steroids are always four fused rings.
Cholesterol is the precursor for all steroid hormones.
Testosterone
Estrogen

61. *IV. Nucleic acids Two types:
a. Deoxyribonucleic acid (DNA- double helix)
b. Ribonucleic acid (RNA-single strand)
Nucleic acids are composed of long chains of nucleotides linked by dehydration synthesis.

62. *Nucleic acids Nucleotides include: phosphate group
pentose sugar (5-carbon)
nitrogenous bases:
adenine (A)
thymine (T) DNA only
uracil (U) RNA only
cytosine (C)
guanine (G)

63. Nucleotide O O=P-O N CH2 O C1 C4 C3 C2 Phosphate Group
Nitrogenous base
(A, G, C, or T)
CH2 O C1 C4 C3 C2 5
Sugar
(deoxyribose)

64. *Nucleotides are bonded to each other by the process of dehydration synthesis, forming phosphodiester bonds.
The arrows in the next slide are pointing to these bonds.

65. DNA - double helix P O 1 2 3 4 5 P O 1 2 3 4 5 G C T A