MACROMOLECULES

1. MACROMOLECULES Carbohydrates and Lipids Mr. Winch Centre Wellington DHS

2. Types of Carbohydrates • Monosaccharides • Oligosaccharides (Di’s and Tri’s) • Polysaccharides

3. “ONE” “SUGAR” “STRAIGHT CHAIN” FORM “RING” FORM (in water) Carbs… Monosaccharides • simple sugar containing 3 to 7 carbons • examples: glucose, fructose, galactose • provides instant energy

4. Start numbering the carbons of your sugars at the end closest to the carbonyl group!!! 1 2 3 4 5 6 1 2 3 4 5 6 Carbs… Characteristics of Sugars 1) An –OH group is attached to each carbon except one; this carbon is double bonded to an oxygen (carbonyl group

5. Carbs… Characteristics of Sugars 2) Size of carbon skeleton varies from 3 to 7 carbons.

6. 1 2 3 4 5 6 1 2 3 4 5 6 Notice how the –OH’s are on different sides. This affects the properties of these molecules & makes them chemically different Carbs… Characteristics of Sugars 3) Spatial arrangements around asymmetric carbon may vary. For example, glucose and galactose are stereoisomers. Can you spot the only difference???

7. The #5C –OH reacts within the molecule at the terminal aldehyde group, breaking the double bond and creates a closed ring 6 5 1 2 3 4 5 6 4 1 2 3 Carbs… Characteristics of Sugars 4) In aqueous solutions, many monosaccharides form rings. Equilibrium favours the ring structure.

8. Carbs… Characteristics of Sugars Figure 7, p. 30 text – Forming α glucose & β glucose

9. MOO!!! Carbs… Dissaccharides “TWO” “SUGARS” • made up of two monosaccharides • common examples: glucose + glucose = maltose (malt sugar) glucose + fructose = sucrose (table sugar) glucose + galactose = lactose (milk sugar)

10. Dissaccharides… cont’d • the forming of a disaccharide creates water in the process - this is known as dehydation synthesis or condensation reaction • the connection between monosaccharides is called a glycosidic linkage

11. Polysaccharides “MANY” “SUGARS” • a complex carbohydrate consisting of many simple sugars linked together

12. Glycogen is a branched polysaccharide. This makes glycogen moreloosely packed, allowing enzymes to access it easily to be broken down into glucose. • Cellulose is tightly packed because of the lack of branches. This allows thecellulose molecules to stack themselves closer to each other, creating bonds between molecules. This causes it to be rigid and makes it difficult to break down.

13. Macromolecule #2LIPIDS Functions: • Long-term energy storage (triglycerides) • Form cell membrane (phospholipids) • Messaging (steroids act as hormones) • Insulation • Cushioning of Internal Organs

14. Lipids Why are lipids well suited for long term energy storage? • Contain many high energy bonds between carbon and hydrogen • Contain twice as much energy per gram than carbohydrates (very concentrated)

15. Types of Lipids • Fats (triglycerides) • Phospholipids • Steroids • Waxes (see text)

16. Fats • Made up of glycerol and 3 fatty acids. • There are many kinds of fatty acids. They differ in two ways: 1. In length 2. In the # of hydrogen atoms attached to it

17. 1 2 3 Glycerol Fatty acids An Example of a Fat Molecule(Triglyceride)

18. triglyceride 3 fattyacids glycerol Digestion of a Fat Molecule + 3 H2O + Fig 1.21 p. 18 The above is a hydrolysis reaction. What is the reverse of this reaction called?

19. Where have you seen these fats? Glycerol + 1 Fatty Acid  Monoglyceride + H2O Glycerol + 2 Fatty Acids  Diglyceride + 2H2O Glycerol + 3 Fatty Acids  Triglyceride + 3H2O

20. Types of Fatty Acids SATURATED (palmitic acid) • No double bonds between carbons MONOUNSATURATED (oleic acid) • 1 double bond POLYUNSATURATED (linoleic acid) • More than 2 double bonds

21. Saturated Unsaturated Polyunsaturated # of double bonds between carbons Orientation State at Room Temp. Origin Which are better for you? Example

22. Types of Fats

23. Types of Fats… cont’d

24. Types of Fats… cont’d

25. Types of Fats… cont’d

26. Types of Fats… cont’d

27. Types of Fats… cont’d

28. What up with TRANS-FATS? • NOT GOOD FOR YOU!!! (FRIES, PEANUT BUTTER) • Created from oils (unsaturated) that are hydrogenated (hydrogen added to double bonds) • Done to increase shelf life, flavour, & workability (eg. semi-solid for baking) • Only partial hydrogenation occurs & get a change in the orientation of hydrogens around some double bonds (cis- turns into trans) • This fat is packaged by your body as LDL (aka BAD cholesterol) leaving you @ risk for heart disease, artheriosclerosis, diabetes & obesity

29. Type of Lipids #2PHOSPHOLIPIDS • are fat derivatives in which one fatty acid has been replaced by a phosphate group and one of several nitrogen-containing molecules. • an important part of the cell membrane (phospholipid bilayer)

30. Phospholipid

31. Phospholipid • The phospholipid can also be represented as: Polar Head – hydrophilic (water-loving) Non-Polar Tails (fatty acids) - hydrophobic (water-hating)

32. Testosterone • Cholesterol • Precursor for other steroids • Component of animal cell membranes • Contributes to arteriosclerosis Type of Lipids #3STEROIDS Steroids consist of 4 fused carbon rings

33. MACROMOLECULES Proteins Mr. Blair Winch Centre Wellington DHS

34. Proteins FUNCTIONS • Act as enzymes (to control chemical reactions) • Provide support and help shape cells • Act as transporters (hemoglobin) • Act as hormones • Make up structures (hair, cartilage) • Act as antibodies (immunoglobulins)

35. Proteins 20 are polymers of… Amino Acids • 8 Essential • Need to obtain via diet • 12 Non-Essential • Body can make

36. R – Side Chain Amino Group Carboxyl Group Central Carbon Amino Acid Structure • R – Side Chain  20 possibilities; different R-groups give the amino acid different biological properties

37. Proteins • Are often very large polymers of many amino acids (monomers) linked together to form POLYPEPTIDES • Proteins are built by condensation reactions forming peptide bonds. aa1 – aa2 dipeptide aa1 – aa2 -- aa3 tripeptide aa1 – aa2 -- aa3 – aan polypeptide • Proteins are broken down through hydrolysis reactions

38. Amino Acid Amino Acid Peptide Bonds (Amide Linkage) Polypeptides Polypeptide Chain Amino Acid • This polypeptide will begin to fold over on itself until it has reached its 3-dimensional shape • The folding will be determined by the R-group interactions of the specific amino acid sequence • It is only the final shape that will determine the protein’s specific function

39. Peptide Bonds + H2O This is a … DEHYDRATION REACTION!

40. Levels of Protein Structure Primary Structure • Amino acid linear sequence Secondary Structure • Folding into a helix or pleated sheet

41. Levels of Protein Structure Tertiary Structure • Folding of secondary structures into a 3-D shape Quarternary Structure • 2 or more polypeptide chains assembling together

42. Hemoglobin – A Complex Protein • Found in RBCs, is responsible for oxygen transport to your cells for respiration • Scientists believe the protein dates back 4 billion years to the start of life • A quarternary protein consisting of 4 polypeptides • 2 of the polypeptides (α subunits) contain 141 amino acids while the other 2 (β subunits) contain 146 amino acids

43. Heme Hemoglobin – A Complex Protein • Heme groups contain iron (II), acting as sites where oxygen molecules can bind

44. DID YOU KNOW? These molecular cages are called porphyrins and are thought to have predated oxygen (2 billion years ago) back when single celled living things used sulfur in its metabolism Hemoglobin – At the Heme of it all

45. MACROMOLECULES Nucleic Acids Mr. Winch Centre Wellington DHS

46. Nucleic Acids • DNA (deoxyribonucleic acid) • RNA (ribonucleic acid) • Nucleotide Triphosphates • Nucleotide Coenzymes

47. DNA and RNA are polymers of… Nucleotides 3 parts Phosphate Pentose sugar Nitrogenous base

48. Basic Nucleotide Structure Purines Pyrimidines

49. Reacting Nucleotides What type of linkage is this? Phosphate ester

50. Key Function of DNA • Store genetic information in an organism Key Function of RNA • Participate in protein synthesis