1. Macromolecules & the Origin of Life
Chapter 3
Macromolecules & the Origin of Life

2. The Molecules of Life Overview:
Another level in the hierarchy of biological organization is reached when small organic molecules are joined together
Atom ---> molecule --- compound

3. Macromolecules Are large molecules composed of smaller molecules
Are complex in their structures
Figure 5.1

4. Macromolecules Most macromolecules are polymers, built from monomers
Four classes of life’s organic molecules are polymers
Carbohydrates
Proteins
Nucleic acids
Lipids

5. Specific monomers make up each macromolecule
A polymer
Is a long molecule consisting of many similar building blocks called monomers
Specific monomers make up each macromolecule
Ex. amino acids are the monomers for proteins

6. The Synthesis and Breakdown of Polymers
Monomers form larger molecules by condensation reactions called dehydration synthesis
(a) Dehydration reaction in the synthesis of a polymer HO H 1 2 3 4
H2O
Short polymer
Unlinked monomer
Longer polymer
Dehydration removes a water molecule, forming a new bond

7. The Synthesis and Breakdown of Polymers
Polymers can disassemble by
Hydrolysis (addition of water molecules)
(b) Hydrolysis of a polymer HO 1 2 3 H 4
H2O
Hydrolysis adds a water molecule, breaking a bond

8. Although organisms share the same limited number of monomer types, each organism is unique based on the arrangement of monomers into polymers
An immense variety of polymers can be built from a small set of monomers

9. Carbohydrates Serve as fuel and building material
Include both sugars and their polymers (starch, cellulose, etc.)

10. Sugars Monosaccharides Are the simplest sugars Can be used for fuel
Can be converted into other organic molecules
Can be combined into polymers

11. Examples of monosaccharides
Triose sugars (C3H6O3)
Pentose sugars (C5H10O5)
Hexose sugars (C6H12O6)
H C OH
H C OH
HO C H
H C OH
C O
HO C H H C O
Aldoses
Glyceraldehyde
Ribose
Glucose
Galactose
Dihydroxyacetone
Ribulose
Ketoses
Fructose

12. Monosaccharides May be linear Can form rings 4C 3 2 OH
H C OH
HO C H
H C O C 1 2 3 4 5 6 OH 4C
6CH2OH 5C
H OH
2 C 1C
3 C 2C
1 C
CH2OH HO
(a) Linear and ring forms. Chemical equilibrium between the linear and ring
structures greatly favors the formation of rings. To form the glucose ring,
carbon 1 bonds to the oxygen attached to carbon 5.

13. Disaccharides
Consist of two monosaccharides
Are joined by a glycosidic linkage

14. Dehydration reaction in the synthesis of maltose
Dehydration reaction in the synthesis of maltose. The bonding of two glucose units forms maltose. The glycosidic link joins the number 1 carbon of one glucose to the number 4 carbon of the second glucose. Joining the glucose monomers in a different way would result in a different disaccharide.
Dehydration reaction in the synthesis of sucrose. Sucrose is a disaccharide formed from glucose and fructose. Notice that fructose, though a hexose like glucose, forms a five-sided ring.
(a)
(b) H HO
H OH OH O
CH2OH
H2O 1 2 4
1– 4 glycosidic linkage
1–2 glycosidic linkage
Glucose
Fructose
Maltose
Sucrose

15. Polysaccharides Polysaccharides Are polymers of sugars
Serve many roles in organisms

16. Storage Polysaccharides
Chloroplast
Starch
Amylose
Amylopectin
1 m
(a) Starch: a plant polysaccharide
Figure 5.6
Starch
Is a polymer consisting entirely of glucose monomers
Is the major storage form of glucose in plants

17. (b) Glycogen: an animal polysaccharide
Consists of glucose monomers
Is the major storage form of glucose in animals
Mitochondria
Giycogen granules
0.5 m
(b) Glycogen: an animal polysaccharide
Glycogen

18. Structural Polysaccharides
Cellulose
Is a polymer of glucose
major component in the rigid cell walls in plants
insoluble and most animals
cannot digest cellulose.
Nutritionally Cellulose is
called fiber or roughage

19. Has different glycosidic linkages than starch
(c) Cellulose: 1– 4 linkage of  glucose monomers H O
CH2OH OH HO 4 C 1
(a)  and  glucose ring structures
(b) Starch: 1– 4 linkage of  glucose monomers
 glucose
 glucose
Figure 5.7 A–C

20. Is a major component of the tough walls that enclose plant cells
Cell walls
Cellulose microfibrils
in a plant cell wall 
Microfibril
CH2OH OH O
Glucose monomer
Parallel cellulose molecules are
held together by hydrogen
bonds between hydroxyl
groups attached to carbon
atoms 3 and 6.
About 80 cellulose
molecules associate
to form a microfibril, the
main architectural unit
of the plant cell wall.
A cellulose molecule
is an unbranched 
glucose polymer.
Cellulose
molecules
Figure 5.8

21. Cellulose is difficult to digest
Cows have microbes in their stomachs to facilitate this process
Figure 5.9

22. Chitin, another important structural polysaccharide
Is found in the exoskeleton of arthropods
Can be used as surgical thread
(a) The structure of the
chitin monomer. O
CH2OH OH H NH C
CH3
(b) Chitin forms the exoskeleton
of arthropods. This cicada
is molting, shedding its old
exoskeleton and emerging
in adult form.
(c) Chitin is used to make a
strong and flexible surgical
thread that decomposes after
the wound or incision heals.
Figure 5.10 A–C

23. Lipids Lipids are a diverse group of hydrophobic molecules Lipids
Are the one class of large biological molecules that do not consist of polymers
Share the common trait of being hydrophobic

24. Fats
Are constructed from two types of smaller molecules, a single glycerol and usually three fatty acids

25. Fats
Vary in the length and number and locations of double bonds they contain

26. (a) Saturated fat and fatty acid
Saturated fatty acids
Have the maximum number of hydrogen atoms possible
Have no double bonds
(a) Saturated fat and fatty acid
Stearic acid
Figure 5.12

27. (b) Unsaturated fat and fatty acid
Unsaturated fatty acids
Have one or more double bonds
(b) Unsaturated fat and fatty acid
cis double bond
causes bending
Oleic acid
Figure 5.12

28. Phospholipids Have only two fatty acids
Have a phosphate group instead of a third fatty acid

29. (a) Structural formula (b) Space-filling model
Phospholipid structure
Consists of a hydrophilic “head” and hydrophobic “tails”
CH2 O P CH C
Phosphate
Glycerol
(a) Structural formula
(b) Space-filling model
Fatty acids
(c) Phospholipid
symbol
Hydrophobic tails
Hydrophilic
head
Hydrophobic
tails –
Hydrophilic head
Choline +
Figure 5.13
N(CH3)3

30. The structure of phospholipids
Results in a bilayer arrangement found in cell membranes
Hydrophilic
head
WATER
Hydrophobic
tail
Figure 5.14

31. Steroids Steroids One steroid, cholesterol
Are lipids characterized by a carbon skeleton consisting of four fused rings
One steroid, cholesterol
Is found in cell membranes
Is a precursor for some hormones HO
CH3
H3C

32. Proteins
Proteins have many structures, resulting in a wide range of functions
Proteins do most of the work in cells and act as enzymes
Proteins are made of monomers called amino acids

33. An overview of protein functions

34. Enzymes
Are a type of protein that acts as a catalyst, speeding up chemical reactions
Substrate
(sucrose)
Enzyme
(sucrase)
Glucose OH
H O
H2O
Fructose
3 Substrate is converted
to products.
1 Active site is available for
a molecule of substrate, the
reactant on which the enzyme acts.
Substrate binds to
enzyme. 2
4 Products are released.

35. Polypeptides Polypeptides A protein
Are polymers (chains) of amino acids
A protein
Consists of one or more polypeptides

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

37. 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

38. 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)

39. Amino Acid Polymers
Amino acids
Are linked by peptide bonds

40. Protein Conformation and Function
A protein’s specific conformation (shape) determines how it functions

41. Four Levels of Protein Structure
Primary structure
Is the unique sequence of amino acids in a polypeptide
Figure 5.20 –
Amino acid subunits
+H3N Amino end o
Carboxyl end c
Gly
Pro
Thr
Glu
Seu
Lys
Cys
Leu
Met
Val
Asp
Ala
Arg
Ser
lle
Phe
His
Asn
Tyr
Trp
Lle

42. Secondary structure
Is the folding or coiling of the polypeptide into a repeating configuration
Includes the  helix and the  pleated sheet O C
 helix
 pleated sheet
Amino acid subunits N H R H
Figure 5.20

43. Is the overall three-dimensional shape of a polypeptide
Tertiary structure
Is the overall three-dimensional shape of a polypeptide
Results from interactions between amino acids and R groups
CH2 CH
O H O C HO
NH3+ -O S
CH3
H3C
Hydrophobic interactions and van der Waals interactions
Polypeptide backbone
Hyrdogen bond
Ionic bond
Disulfide bridge

44. Quaternary structure
Is the overall protein structure that results from the aggregation of two or more polypeptide subunits
Polypeptide chain
Collagen
 Chains
 Chains
Hemoglobin
Iron
Heme

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

46. Sickle-Cell Disease: A Simple Change in Primary Structure
Results from a single amino acid substitution in the protein hemoglobin

47. Sickle-cell hemoglobin
Primary structure
Secondary and tertiary structures
Quaternary structure
Function
Red blood cell shape
Hemoglobin A
Molecules do not associate with one another, each carries oxygen.
Normal cells are full of individual hemoglobin molecules, each carrying oxygen  
10 m
Hemoglobin S
Molecules interact with one another to crystallize into a fiber, capacity to carry oxygen is greatly reduced.
 subunit 1 2 3 4 5 6 7
Normal hemoglobin
Sickle-cell hemoglobin
. . .
Figure 5.21
Exposed hydrophobic region
Val
Thr
His
Leu
Pro
Glul
Glu
Fibers of abnormal hemoglobin deform cell into sickle shape.

48. What Determines Protein Conformation?
depends on the physical and chemical conditions of the protein’s environment
Temperature, pH, etc. affect protein structure

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

50. The Protein-Folding Problem
Most proteins
Probably go through several intermediate states on their way to a stable conformation
Denatured proteins no longer work in their unfolded condition
disruption and possible destruction of both the secondary and tertiary structures.
Proteins may be denatured by extreme changes in pH or temperature

51. Chaperonins
Are protein molecules that assist in the proper folding of other proteins
Hollow cylinder
Cap
Chaperonin (fully assembled)
Steps of Chaperonin Action: An unfolded poly- peptide enters the cylinder from one end.
The cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide.
The cap comes off, and the properly folded protein is released.
Correctly folded protein
Polypeptide 2 1 3
Figure 5.23

52. Nucleic Acids Nucleic acids store and transmit hereditary information
Genes
Are the units of inheritance
Program the amino acid sequence of polypeptides
Are made of nucleotide sequences on DNA

53. The Roles of Nucleic Acids
There are two types of nucleic acids
Deoxyribonucleic acid (DNA)
Ribonucleic acid (RNA)

54. Synthesis of mRNA in the nucleus
DNA Functions
Stores information for the synthesis of specific proteins
Found in the nucleus of cells
Directs RNA synthesis (transcription)
Directs protein synthesis through RNA (translation) 1 2 3
Synthesis of mRNA in the nucleus
Movement of
mRNA into cytoplasm
via nuclear pore
Synthesis
of protein
NUCLEUS
CYTOPLASM
DNA
mRNA
Ribosome
Amino acids
Polypeptide

55. The Structure of Nucleic Acids
5’ end
5’C
3’ end OH O
Nucleic acids
Exist as polymers called polynucleotides
Each polynucleotide
Consists of monomers called nucleotides
(Sugar + phosphate + nitrogen base)
Nitrogenous
base
Nucleoside O O O P
CH2
5’C
3’C
Phosphate
group
Pentose
sugar

56. (c) Nucleoside components
Nucleotide Monomers
Nucleotide monomers
Are made up of nucleosides (sugar + base) and phosphate groups CH
Uracil (in RNA) U
Ribose (in RNA)
Nitrogenous bases Pyrimidines C N O H
NH2 HN
CH3
Cytosine
Thymine (in DNA) T HC NH
Adenine A
Guanine G
Purines
HOCH2 OH
Pentose sugars
Deoxyribose (in DNA) 4’ 5” 3’ 2’ 1’
Figure 5.26
(c) Nucleoside components

57. Nucleotide Polymers Nucleotide polymers
Are made up of nucleotides linked by the–OH group on the 3´ carbon of one nucleotide and the phosphate on the 5´ carbon on the next

58. Gene The sequence of bases along a nucleotide polymer
Is unique for each gene

59. The DNA Double Helix Cellular DNA molecules
Have two polynucleotides that spiral around an imaginary axis
Form a double helix

60. The DNA double helix Consists of two antiparallel nucleotide strands
3’ end
Sugar-phosphate backbone
Base pair (joined by hydrogen bonding)
Old strands
Nucleotide about to be added to a new strand A
5’ end
New strands

61. A,T,C,G The nitrogenous bases in DNA
Form hydrogen bonds in a complementary fashion (A with T only, and C with G only)