1. The Structure and Function of Macromolecules

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

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

4. 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
Figure 5.2A

5. 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
Figure 5.2B

6. Carbohydrates
Serve as fuel (like glucose/sugars) and building material (like cellulose) and a carbon source, and storage (starch)

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

8. 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
Figure 5.3

9. Monosaccharides May be linear Can form rings (more common) 4C OH 3 2 H
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

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

11. Figure 5.5 CH2OH O H H OH HO OH H2O
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
Figure 5.5

12. Polysaccharides Polysaccharides Are polymers of sugars
Serve many roles in organisms such as storage of glucose and for structure

13. 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 (like in peas)

14. (b) Glycogen: an animal polysaccharide
Glycogen - a storage polysaccharide
Consists of glucose monomers
Is the major storage form of glucose in animals (like in us)
Mitochondria
Giycogen granules
0.5 m
(b) Glycogen: an animal polysaccharide
Glycogen
Figure 5.6

15. Cellulose - structural polysaccharide
major component of the tough walls that enclose plant cells
Plant cells
0.5 m
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

16. Cellulose (also known as dietary fiber) is difficult to digest
Cows have microbes in their stomachs to facilitate this process
Fiber stimulates our digestive tract to make mucus and keep things moving along
Figure 5.9

17. Lipids
Lipids are a diverse group of hydrophobic molecules (water hating)
The nonpolar bond between Carbon and Hydrogen make the molecules nonpolar
These are fats, oils, waxes, phospholipids, and steroids.
Biological functioning: part of membranes, energy storage, cell signaling, vitamins A, D, E, and K are fat soluble and stored in adipose (fatty tissue)

18. Fats
Are constructed of a single glycerol and usually three fatty acids (sometimes called triglycerides)
Vary in the length and number and locations of double bonds they contain

19. (a) Saturated fat and fatty acid
Saturated fats (saturated fatty acids)
Saturated with hydrogens
Have no carbon-carbon double bonds
(a) Saturated fat and fatty acid
Stearic acid
Figure 5.12

20. (b) Unsaturated fat and fatty acid
Unsaturated fats (oils)
Have one or more carbon-carbon double bonds (Omega 3 and Omega 6)
(b) Unsaturated fat and fatty acid
cis double bond
causes bending
Oleic acid
Figure 5.12

21. Trans fats are fats that have a double bond on the trans side of the molecule (meaning that the hydrogens are on opposite sides)
Cis Fat Trans fat

22. (a) Structural formula (b) Space-filling model
Phospholipids
Consists of a hydrophilic “head” and 2 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

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

24. Steroids (like cholesterol) are lipids with a four carbon ring
Many hormones are synthesized from cholesterol in our liver HO
CH3
H3C
Figure 5.15

25. 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

26. An overview of protein functions
Table 5.1

27. 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.
Figure 5.16

28. Polypeptides Polypeptides
Are polymers (chains) of amino acids joined by peptide bonds
Amino acid polypeptideprotein

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

30. 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

31. 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)

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

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

34. 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

35. Includes the  helix and the  pleated sheet
Secondary structure
Is the folding or coiling of the polypeptide into a repeating configuration
Includes the  helix and the  pleated sheet
Folding is due to several things (ex. Affinity for oxygen) O C
 helix
 pleated sheet
Amino acid subunits N H R H
Figure 5.20

36. 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

37. 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

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

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

40. 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.

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

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

43. The Protein-Folding Problem
Most proteins
Probably go through several intermediate states on their way to a stable conformation
Denaturated proteins no longer work in their unfolded condition
Proteins may be denaturated by extreme changes in pH or temperature

44. 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

45. X-ray crystallography
Is used to determine a protein’s three-dimensional structure
X-ray diffraction pattern
Photographic film
Diffracted X-rays
X-ray source
X-ray beam
Crystal
Nucleic acid
Protein
(a) X-ray diffraction pattern
(b) 3D computer model
Figure 5.24

46. 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

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

48. Deoxyribonucleic Acid
DNA
Stores information for the synthesis of specific proteins
Found in the nucleus of cells

49. Synthesis of mRNA in the nucleus
DNA Functions
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
Figure 5.25

50. The Structure of Nucleic Acids
5’ end
5’C
3’ end OH
Figure 5.26 O
Nucleic acids
Exist as polymers called polynucleotides
(a) Polynucleotide,
or nucleic acid

51. 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
(b) Nucleotide
Figure 5.26

52. (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

53. 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

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

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

56. 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
Figure 5.27

57. 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)

58. DNA and Proteins as Tape Measures of Evolution
Molecular comparisons
Help biologists sort out the evolutionary connections among species

59. The Theme of Emergent Properties in the Chemistry of Life: A Review
Higher levels of organization
Result in the emergence of new properties
Organization
Is the key to the chemistry of life