2. Chapter 5: Macromolecules

3. Macromolecules A large molecule in a living organism –Proteins, Carbohydrates, Nucleic Acids Polymer- long molecules built by linking repeating building blocks in a chain Monomer- units that serve as building blocks of polymer

4. Dehydration Synthesis -How cells link together monomers -Monomers have H atoms and hydroxyl groups -Add a monomer to a chain, a water molecule is released

5. Hydrolysis -Opposite of dehydration synthesis -Bond in a polymer are broken by addition of water

6. 1. Carbohydrates Carbohydrates: include sugars and polymers of sugar Monosaccharides: the simplest carbohydrate, made of a single sugar

7. Monosaccharides The simplest carbohydrate made of a single sugar Have molecular formulas multiple of CH 2 0 (Most common sugar is glucose C 6 H 12 0 6 ) Have a hydroxyl group (OH) and a carbonyl group (C=0) OH group make it an alcohol and the C=0 make it an aldehyde or ketone

8. Fig. 5-3 Dihydroxyacetone Ribulose Ketoses Aldoses Fructose Glyceraldehyde Ribose Glucose Galactose Hexoses (C 6 H 12 O 6 ) Pentoses (C 5 H 10 O 5 ) Trioses (C 3 H 6 O 3 )

9. Though often drawn as linear skeletons, in aqueous solutions many sugars form rings Monosaccharides serve as a major fuel for cells (glucose) Most sugars end in -ose Monosaccharides (cont’d)

10. Disaccharide A double sugar created when dehydration synthesis joins Ex: 2 glucose -> maltose (malt sugar makes beer) Glycosidic linkage: covalent bond between 2 sugars of a disaccharide

11. (b) Dehydration reaction in the synthesis of sucrose GlucoseFructose Sucrose MaltoseGlucose (a) Dehydration reaction in the synthesis of maltose 1–4 glycosidic linkage 1–2 glycosidic linkage

12. Many act as storage molecules of sugar, that cells break down for energy Hundreds or thousands of monosaccharides joined together (glycosidic links) Polysaccharide

13. Polysaccharide- Starch Made of all glucose and found in plants Plants store starch and break into glucose when needed for energy Humans and animals hydrolyze starch when they eat it (found in wheat, corn, rice, potatoes)

15. Glycogen is hydrolyzed to release glucose when needed Excess sugar in animals is stored as glycogen in liver and muscles Polysaccharide- Glycogen

16. A component of a plant’s cell wall, gives them structure Polysaccharide- Cellulose Cellulose molecules connected by hydrogen bonds and form fiber

17. Fig. 5-9

18. Chitin, another structural polysaccharide, is found in the exoskeleton of arthropods Chitin also provides structural support for the cell walls of many fungi Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

19. Fig. 5-10 The structure of the chitin monomer. (a) (b) (c) Chitin forms the exoskeleton of arthropods. Chitin is used to make a strong and flexible surgical thread.

20. What does this say about their solubility? Compounds that consist mainly of C and H atoms linked by nonpolar covalent bonds Lipid Ex: fats, oils, cholesterol, waxes

21. - a 3 carbon alcohol with hydroxyl group A large lipid made of glycerol and fatty acids Fats Ex: fats, oils, waxes 1 fat molecule = 1 glycerol and 3 fatty acids Function is energy storage (1 g of fat stores more than 2x as much energy as 1 g of starch)

22. Fig. 5-11 Fatty acid (palmitic acid) Glycerol (a) Dehydration reaction in the synthesis of a fat Ester linkage (b) Fat molecule (triacylglycerol)

23. No double bond in fatty acid Solids (lard, butter- animal fats) Leads to heart disease, plaque in blood vessels Saturated Fats

24. the fatty acid contains double bonds, preventing the skeleton from having the max # of hydrogen’s. Molecules can’t pack together tightly and form liquids at room temp (oils and plant fats) Unsaturated Fats

25. The Curious Case of Olestra

26. A diet rich in saturated fats may contribute to cardiovascular disease through plaque deposits Hydrogenation is the process of converting unsaturated fats to saturated fats by adding hydrogen Hydrogenating vegetable oils also creates unsaturated fats with trans double bonds These trans fats may contribute more than saturated fats to cardiovascular disease Copyright © 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings

27. Major component of cell membranes Similar to fat, but contain phosphorus and have 2 fatty acid (not 3) Phospholipids

28. Cholesterol Stabilizes cell membrane Helps resist temperature changes

29. 1 fatty acid and an alcohol More hydrophobic than fats Natural coating on fruit Insects have to keep from drying out Waxes

30. lipids whose carbon skeleton is bent to form 4 fused rings all steroids have 3-6 sided rings and 1-5 sided ring Ex: cholesterol found in animal cell membranes and animal cells use it to make other steroids (estrogen and testosterone) Steroids

31. Fig. 5-15

32. Chapter 5: Macromolecules http://www.youtube.com/watch? v=lijQ3a8yUYQ

33. Proteins Proteins account for more than 50% of the dry mass of most cells Protein functions include structural support, storage, transport, cellular communications, movement, and defense against foreign substances

34. Table 5-1

35. Enzymes are a type of protein that acts as a catalyst to speed up chemical reactions Enzymes can perform their functions repeatedly being reused Enzymes

36. Fig. 5-16 Enzyme (sucrase) Substrate (sucrose) Fructose Glucose OH H O H2OH2O

37. Amino Acid Monomers Amino acids (monomers) build proteins (polymers) Amino acids are organic molecules with carboxyl and amino groups Amino acids differ in their properties due to differing side chains, called R groups THE R GROUP is the variable part of the amino acid and determines physical and chemical properties

38. Fig. 5-UN1 Amino group Carboxyl group  carbon

39. Nonpolar Glycine (Gly or G) Alanine (Ala or A) Valine (Val or V) Leucine (Leu or L) Isoleucine (Ile or I) Methionine (Met or M) Phenylalanine (Phe or F) Trypotphan (Trp or W) Proline (Pro or P) Polar Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine (Asn or N) Glutamine (Gln or Q) Electrically charged AcidicBasic Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H)

40. Fig. 5-17c Acidic Arginine (Arg or R) Histidine (His or H) Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Basic Electrically charged

41. Amino Acid Polymers Amino acids are linked by peptide bonds between carbonyl and amino group A polypeptide is a polymer of amino acids Polypeptides range in length from a few to more than a thousand monomers Each polypeptide has a unique linear sequence of amino acids

42. Peptide bond Fig. 5-18 Amino end (N-terminus) Peptide bond Side chains Backbone Carboxyl end (C-terminus) (a) (b)

43. Polypeptides Polypeptides are polymers built from the same set of 20 amino acids A protein consists of one or more polypeptides

44. Protein Structure and Function A functional protein consists of one or more polypeptides twisted, folded, and coiled into a unique shape

45. The sequence of amino acids determines a protein’s three-dimensional structure A protein’s structure determines its function

46. Primary structure, the sequence of amino acids in a protein, is like the order of letters in a long word Primary structure is determined by inherited genetic information Primary Structure

47. The coils and folds of secondary structure result from hydrogen bonds between repeating constituents of the polypeptide backbone (amino and carbonyl group Typical secondary structures are a coil called an alpha helix and a folded structure called a pleated sheet Secondary Structure

48. Tertiary structure is determined by interactions between R groups, rather than interactions between backbone constituents These interactions between R groups include hydrogen bonds, ionic bonds, hydrophobic interactions, and van der Waals interactions Strong covalent bonds called disulfide bridges may reinforce the protein’s structure Tertiary Structure

49. Fig. 5-21e Tertiary StructureQuaternary Structure

50. Fig. 5-21f Polypeptide backbone Hydrophobic interactions and van der Waals interactions Disulfide bridge Ionic bond Hydrogen bond

51. Quaternary structure results when two or more polypeptide chains form one macromolecule Forms a “globular protein” Quaternary Structure

52. Fig. 5-21g Polypeptide chain  Chains Heme Iron  Chains Collagen Hemoglobin

53. Sickle-Cell Disease: A Change in Primary Structure A slight change in primary structure can affect a protein’s structure and ability to function Sickle-cell disease, an inherited blood disorder, results from a single amino acid substitution in the protein hemoglobin

54. What Determines Protein Structure? In addition to primary structure, physical and chemical conditions can affect structure Alterations in pH, salt concentration, temperature, or other environmental factors can cause a protein to unravel This loss of a protein’s structure is called denaturation A denatured protein is biologically inactive

55. Fig. 5-23 Normal protein Denatured protein Denaturation Renaturation

56. The Roles of Nucleic Acids There are two types of nucleic acids: –Deoxyribonucleic acid (DNA) –Ribonucleic acid (RNA) DNA provides directions for its own replication DNA directs synthesis of messenger RNA (mRNA) and, through mRNA, controls protein synthesis Protein synthesis occurs in ribosomes

57. Fig. 5-26-3 mRNA Synthesis of mRNA in the nucleus DNA NUCLEUS mRNA CYTOPLASM Movement of mRNA into cytoplasm via nuclear pore Ribosome Amino acids Polypeptide Synthesis of protein 1 2 3

58. The Structure of Nucleic Acids Nucleotides are monomers of DNA/RNA Each nucleotide consists of a nitrogenous base, a pentose sugar, and a phosphate group

59. Nucleotide Polymers Adjacent nucleotides are joined by covalent bonds These links create a backbone of sugar-phosphate units