1. The Chemistry of Carbon = Chemistry of Life
3.2: Carbon Compounds
All of the many compounds can be classified in TWO broad categories:
ORGANIC COMPOUNDS AND
INORGANIC COMPOUNDS.
ORGANIC CHEMISTRY =
The Chemistry of Carbon =
Chemistry of Life

2. ORGANIC
Made up of mostly what element?
CARBON
-C-C-C-C-C-C-C-C

3. II. Carbon’s Bonding Behavior
A. Outer shell of carbon has ____ electrons; but can hold ____
B. Each carbon atom can form __________ bonds with up to _________ atoms 4 8
covalent
four

4. 4 covalent bonds C

5. rings chains backbone Functional groups
C. Carbon atoms can form _______________ or ______________
D. Carbon atoms covalently bonded form the ________________ of organic compounds
E. ______________ can project from the carbon backbone
rings
chains
backbone
Functional groups

6. F. Carbon’s tendency to _______________ results in an enormous variety of ORGANIC COMPOUNDS
Carbon can share two or even three pair of electrons with another atom
    a) SINGLE BOND - A bond formed when two atoms share ONE pair of electrons.
    b) DOUBLE BOND - Atoms share TWO pairs of electrons.
    c) TRIPLE BOND - Atoms Sharing THREE pairs of electrons.
bond with itself

7. Covalent Bonds – single, double, triple

8. C C

9. III. Functional Groups carbon backbone
A. Atoms or clusters of atoms that are covalently bonded to a _____________________________
B. Gives organic compounds their different properties
ex: HYDROXYL GROUP -OH attached
makes an ALCOHOL
carbon backbone

10. Examples of Functional Groups
Hydroxyl group - OH
Amino group - NH3+
Carboxyl group - COOH
Phosphate group - PO3-
Methyl group - CH3

11. R – Is a repeating unit

12. IV. LARGE CARBON MOLECULES
Large Carbon Compounds are built up from smaller simpler molecules called _______________ (building blocks)
(MONO = ONE)
B. Monomers can bind to one another to form complex molecules known as
_________________
(POLY = MANY)
C. A Polymer consist of repeated, linked units, forming large polymers called ______________________
(MACRO = LARGE)
MONOMERS
POLYMERS
MACROMOLECULES

13. 1. Condensation-Dehydration Synthesis
V. Types of Reactions
1. Condensation-Dehydration Synthesis
2. Hydrolysis

14. polymers -OH H 1) Condensation Reactions (Dehydration Synthesis)
a) Monomers link to form ______________ 
b) Monomers are CONDENSED and water (H2O) is squeezed out (DEHYDRATE)
-H2O is a by-product of the reaction
c) Enzymes remove from one molecule, from another
 bond formed between two molecules
polymers
-OH H

15. Visualize! CONDENSATION (dehydration synthesis)
enzyme action at functional groups
Visualize!
Fig. 3.4a, p. 37

16. 2) Hydrolysis BREAKDOWN
a) The _________________ of complex molecules, such as polymers
b) SPLITTING of a WATER molecule to ADD -OH group and an H
 bonds break that hold polymers together
BREAKDOWN

17. enzyme action at functional groups
HYDROLYSIS
enzyme action at functional groups
Visualize!
Fig. 3.4b, p. 37

18. 3.3 MOLECULES OF LIFE
Four organic compounds:
Carbohydrates
Proteins
Lipids
Nucleic Acids
Plants: mostly carbs
Animal: mostly protein

19. What is the difference between structural formula and molecular formula?
Molecular Formula: H2O
The way it is written
Structural Formula: H – O – H
The way it looks (arrangement)

20. Human Body CHON! Oxygen 65% Carbon 18% Hydrogen 10% Nitrogen 3%
Calcium %
Phosphorus %
Sulfur %
Sodium %
Chlorine %
Magnesium
Iron %
CHON!

21. 1. Carbohydrates: sugars and starches
contain C, H, and O in the ratio of CH2O
-carbo (C) hydrate (H2O)
a) monomers of sugars (simple sugars) -
Monosaccharides

22. 1)eg: Glucose (manufactured by plants) Fructose (found in fruits)
2) ____________: has the same molecular formula but a different structural formula
3) Used for _______________________
ISOMER
quick energy

23. Isomers: same molecular formula, but different structural formula
glucose
fructose
galactose

24. b) Disaccharides – double sugar C6H12O6 + C6H12O6 = C12H22O11 + H2O
What type of reaction??
dehydration synthesis – combining of 2 monomers (monosaccharides) by squeezing out a H20
1) EXAMPLES:
sucrose (glucose + fructose = table sugar)
maltose (2 glucose)
2) bond between two monosaccharides is called a ___________________ bond
3) a disaccharide contains __________energy than the two units it is composed of (bc of bond)
glycosidic
more

25. Disaccharides Made up of? What type of bond? What type of reaction?
Two monosaccharides
What type of bond?
Covalent
“Glycosidic”
What type of reaction?
condensation reaction (dehydration synthesis)
glucose
fructose
+ H2O
sucrose

28. Other sugars:
MONOSACCHARIDES OR DISACCHARIDES?

29. Polysaccharides glucose macromolecule glycogen
c) _________________ – 3 or more monosaccharides
complex carbohydrates, starches, cellulose, chitin
1) most abundant of carbohydrates
2) thousands of _____________ units bonded together by dehydration synthesis =
type of: ____________________________
3) energy storage molecules
plants = starch
animals = “animal starch”
glucose
macromolecule
glycogen

30. structural also important as _____________ components of organisms:
eg. -cellulose = 50% of carbon in plants
-chitin = exoskeleton of insects
structural

31. Glycogen animals muscle liver breakdown glucose
Sugar storage form in _____________
Large storage in _______ and _______ cells
When blood sugar decreases,
liver cells _____________ glycogen,
releasing _____________
muscle
liver
breakdown
glucose

32. larger molecules will not “leak” out of cells
cells store energy as polysaccharides rather than glucose units because the
_________________________________
(warehouse of simple sugars)
larger molecules will not “leak” out of cells

33. Cellulose and Starch
plant cell wall
plant energy storage

34. (celery strings)

35. Cellulose & Starch Differ in bonding patterns between monomers
Cellulose - tough, indigestible, structural material in plants (corn covering )
Starch - easily digested, storage form in plants (potato insides)

36. 2 Examples of MONOSACCHARIDE
GLUCOSE
FRUCTOSE

37. Example of DISACCHARIDE
SUCROSE
(Glucose + Fructose)

38. 4 examples of POLYSACCHARIDES stores energy: makes up stuff:
CELLULOSE
CHITIN (on insects)
STARCH
GLYCOGEN
plants
animals

39. 2. Lipids water soap A) Composed of C, H, and O
b) Ratio of C to H to O higher than in carbohydrates
c) Defined based on their solubility:
1) they are insoluble in ___________
2) they are soluble in ____________
Primary function –
to store large amounts of energy
(twice as much energy as carbs and proteins
water
soap

40. e) Secondary functions of lipids: structural components
eg. phospholipids- major building block in cell membranes
2. "messengers" (hormones) that play roles in communications within and between cells
(can’t dissolve in blood plasma  protects message)
3. insulation and padding

41. fatty acids Monomers of Lipids are:
3 fatty acids covalently bonded to a 3-carbon “backbone”-
The fatty acids are composed of CH2 units
fatty acids
glycerol

42. Fatty Acids building blocks of: (fats, waxes, phospholipids, but not sterols)
1) Carboxyl group (-COOH) at one end
Methyl (CH3 ) group at the other end
2) Carbon (CH2) backbone (up to 36 C atoms)

43. Single
Saturated - __________ bonds between carbons
_________ at room temperature
5) Unsaturated – One ________ bond ________ at room temperature
Polyunsaturated – more than one __________ bond
_________ at room temp.
solid
double
liquid
double
liquid

44. Three Fatty Acids
stearic acid
oleic acid
linolenic acid S PU U

45. 7) Glycerol backbone – fatty acids attach to the glycerol
Dehydration synthesis removes the –H from the glycerol and -OH from the fatty acid to form a glycosidic bond.

46. Triglyceride formed by dehydration synthesis
glycerol
three fatty acid tails
triglyceride
Fig. 3.8b, p. 40

47. Unsaturated Fat

49. Alpha end – from carboxyl Omega end – from methyl # - which carbon has double bond

50. TRANS UNSATURED FAT CIS-UNSATURATED SATURATED FAT
EASIEST TO BREAKDOWN 
USUALLY ARTIFICIAL 

51. 9) Phospholipids Main components of cell membranes
Phosphate group
Main components of cell membranes
Has a phosphate group and two fatty acids

52. Phospholipid

54. Phospholipid Bilayer

56. Waxes Long-chain fatty acids linked to carbon RINGS
Feels hard, REPEL water
Important in water-proofing

60. Sterols and steroids No fatty acids
Rigid backbone of four fused-together carbon rings
Cholesterol - most common type in animals

61. Low-density lipoproteins (barely moves fats around)
High-density lipoproteins (efficiently moves fats around) 

62. LE 4-9
Estradiol
Female lion
Testosterone
Male lion

63. Transgender -one's gender identity not matching one’s assigned sex
Heterosexual – into opposite sex
Homosexual – into same sex
Bisexual – into both sexes
Androgenous – combo of male and female char
Hermaphrodite – having both sexual organs
Transvestite - dress or act like opposite sex

64. 3. Nucleic Acids nucleotides DNA strand  Include DNA and RNA
What are the monomers of nucleic acids?
DNA strand 
nucleotides

65. DNA 
Holds genetic info
RNA 
Holds instructions to make proteins

66. Nucleotide Structure Sugar Phosphate group Nitrogen Base
Ribose or deoxyribose
Phosphate group
Nitrogen Base

67. Nucleic Acids Composed of nucleotides Single- or double-stranded
Adenine
Cytosine
Composed of nucleotides
Single- or double-stranded
Sugar-phosphate backbone

68. three phosphate groups
ATP - A Nucleotide
base
three phosphate groups
sugar

69. Adenosine Triphosphate
ATP
Adenosine Triphosphate
= ATP
- energy currency of cell
A. Temporarily stores large amounts of energy in phosphate bonds
B. Regulates many biological pathways
C. is made in a process called
cellular respiration

70. D. ATP is a monomer of __________ made up of three components
nucleic acids
1) = nitrogen containing base
Adenine

71. 2) = 5 carbon sugar
Ribose
C5H10O5

72. 3) 3 inorganic (from phosphoric acid)
phosphate groups
3) 3 inorganic (from phosphoric acid)

73. three phosphate groups
ATP - A Nucleotide
base
three phosphate groups
sugar
animation

75. How ATP releases ENERGY
phosphate
When break a ______________ group off by _________________
It becomes  _______ (adenosine DIphosphate
And ___________________ energy
hydrolysis
ADP
releases

76. Adenosine diphosphate
II = ADP
A. Adenine - ribose- P ~ P
B. When the last phosphate group is released from ATP, ADP is formed.
ATP ----> ADP P
energy

77. Why would you need ENERGY from ATP in a cell?
build larger molecules
carry substances into the cell
remove wastes from the cell
for mechanical work (like muscular activity).

78. 4. Proteins
A. Most complex and important substances in living organisms
B. Composed of C, H, O, N
Monomer of a protein is:
amino acid

79. Types/FUNCTION of Proteins:
1) structural (makes up) – parts of cells, tissues, collagen and elastin

80. What is COLLAGEN? 1/4 of protein in bodies ! Makes up 75% of our SKIN
Also makes up cartilage, bone..etc.
BOTOX, lip injections…etc 

82. 2) Transport/contractile –in muscle; myosin and actin -in cell membrane; calcium pump

83. 3) Communication/hormones – insulin -growth factor

84. Storage -ferritin (stores iron from our food)

85. Defense – immunoglobin -antibodies

86. enzymes – largest group of proteins; regulate reactions (organic catalyst) -alpha amylase

87. E. Amino Acid R group – 20 different kinds with distinct properties
Stupid lil H
amino
group
carboxyl
group
R group – 20 different kinds with distinct properties

88. 1) Properties of Amino Acids
a) Determined by the “R group”
b) there are 20 different Amino Acids
c) Amino acids may be:

89. where are the R groups? valine (val) tyrosine (tyr) lysine (lys)
glutamate (glu)
glycine (gly)
where are the R groups?
valine (val)
phenylalanine (phe)
methionine (met)
proline (pro)
Fig. 3.12, p. 42

90. 2) Protein Synthesis
A Protein is a chain of amino acids linked by peptide bonds
Peptide bond:
Type of covalent bond
Links amino group of one amino acid with carboxyl group of next
Forms through condensation reaction (dehydration synthesis)

91. C - N - C
newly
forming
polypeptide
chain
Fig. 3.14, p. 43

92. The sequence (arrangement) of amino acids
If there are only 20 amino acids, how are there so many types of proteins?
The sequence (arrangement) of amino acids
The kinds of amino acids present
The number of amino acids in a protein

93. -N-C-C-N-C-C-N-C-C-N-
Protein Synthesis
Two linked amino acids = dipeptide
Three or more amino acids= polypeptide
Protein – two or more polypeptide chains
Backbone of polypeptide has N atoms:
-N-C-C-N-C-C-N-C-C-N-

94. Protein Shapes Globular proteins Fibrous proteins
Polypeptide chains arranged as strands or sheets
Globular proteins
Polypeptide chains folded into compact, rounded shapes

95. 1-Primary Structure & Protein Shape
Long strand of protein

96. 2-Secondary Structure (twisted)

97. 3-Tertiary Structure
heme group
Folding as a result of interactions between R groups
coiled and twisted polypeptide chain of one globin molecule

98. 4-Quaternary Structure
Some proteins are made up of more than one polypeptide chain
Hemoglobin

100. Denaturation Disruption of three-dimensional shape
Breakage of weak bonds
Causes of denaturation: pH
Temperature
Destroying protein shape disrupts function

101. fever!

102. What’s a REALLY IMPORTANT protein that speeds up reactions by either breaking or making things?
ENZYMES

103. Copy into notes p.4 at bottom:
active site
ES complex
substrate
enzyme
enzyme
products

105. Enzymes LOWER Activation Energy
without enzyme
starting
substance
activation energy
with enzyme
energy
released
by the
reaction
products

106. Enzymes
Are Catalysts found in organisms (biological/organic catalysts)
Name based on compound being affected. Most end in “ase”:
- Lipase (works on lipids)
- Maltase (works on maltose)
- Lactase (works on lactose)
- protease (works on proteins)

107. AMYLASE – breaks down starch
Where is it found in your body?

108. Catalase The Bombardier Beetle
Catalyzes the formation of oxygen and water from hydrogen peroxide
2H2O > 2H2O + O2
The Bombardier Beetle

109. Every enzyme has one or more active sites. “breaking” reaction

110. Visualize!

111. Effect of Temperature What does cold temperatures do to enzymes?
What does warm temperature do to enzymes?
What do REALLY high temperatures do to enzymes?

112. Effect of pH

113. LOCK AND KEY MODEL INDUCED FIT MODEL
substrates fits into the active site like a key fits into a lock
INDUCED FIT MODEL
substrates fits into the active site by deforming it somewhat

114. Induced-Fit Model “making” reaction two substrate molecules substrates
contacting
active site
of enzyme
“making” reaction
active sight
TRANSITION
STATE
(tightest
binding but
least stable)
end
product
enzyme
unchanged
by the
reaction

115. COUPLED REACTION = BIOCHEMICAL PATHWAY

116. Competitive Inhibitors
In competitive inhibition, an INHIBITOR can block the active site so the SUBSTRATE can’t fit there

117. Non-Competitive Inhibition
Non-competitive inhibitors do not compete with active site, but stick to enzyme somewhere else and changes enzyme’s shape so substrate can’t fit

118. Where do we get our enzymes from?
VITAMINS!

119. Vitamin B5 (panthenol) becomes Coenzyme-A and moves acetyl groups CH3CO- about in respiration.
Vitamin B2 (riboflavin) becomes flavin mononucleotide (FADH2) and moves electrons about in respiration.
Vitamin B12 (cobalamin) becomes bound moves methyl CH3- groups about in the C1 metabolism (important for nucleotide synthesis).
Vitamin C (ascorbate) moves electrons onto Fe3+ ion in prolyl hydroxylase, which is needed for collagen synthesis, hence the symptoms of scurvy (soggy gums).

120. Factors Influencing Enzyme Activity
Temperature pH
Reusability
Salt concentration