2. MOLECULES of life

4. And.. What we fart!

6.  Organic Compounds contain Carbon.  Carbon is an important element because… It forms 4 bonds. Tends to form strong covalent bonds.

7.  Can combine to form:  single, double & triple bonds as well as  chains  branches and rings.

8.  We will practice building these today!

9.  Functional groups help determine properties of organic compounds  All are polar because oxygen or nitrogen exert a strong pull on shared electrons  Polarity tends to make these molecules hydrophilic (water-loving) A necessity for life!

10. X

11.  Activity 3B – online textbook Activity 3B – online textbook

12.  There are 4 major categories of organic compounds: Carbohydrates Lipids Proteins Nucleic Acids

13.  Carbohydrates, Lipids, Proteins and Nucleic Acids are macromolecules.  This means they are BIG molecules.

14.  They are made of smaller molecules that serve as the building blocks.  Like a brick is the building block for a brick wall these smaller molecules combine to create the macromolecules.

15.  Smaller Molecules (Building Blocks/subunits) = monomers  Larger Molecules = polymers

16. Condensation Reaction /Dehydration Synthesis Hydrolysis Reaction MonomerPolymer Remove water Add water

17. Removing water to build a polymer

18. Adding water to break down a polymer

19.  Why does our body (and all living things) need this molecule?  Provides ENERGY  Where do we get this molecule?  Pasta, Potatoes, Rice, Candy, Soda, Sugar

20. Which is the polymer and which is the monomer? Polymer! Monomer!

21.  Monomers of carbs = monosaccharide  Mono means 1, saccharide means sugar  Common examples are: Glucose (grains) Fructose (fruit) Galactose (milk)

22. C C C C C C C C C C H H H H H H H H H H H HOHO H H H C O HO OHOH OHOH OHOH OHOH OHOH OHOH OHOH C O OHOH Glucose Fructose

23. C C C C C C C C C C H H H H H H H H H H H HOHO H H H C O HO OHOH OHOH OHOH OHOH OHOH OHOH OHOH C O OHOH Glucose Fructose

24. C C C C C C C C C C H H H H H H H H H H H HOHO H H H C O HO OHOH OHOH OHOH OHOH OHOH OHOH OHOH C O OHOH Glucose Fructose GlucoseFructose Carbon66 Hydrogen12 Oxygen66

25. C C C C C C C C C C H H H H H H H H H H H HOHO H H H C O HO OHOH OHOH OHOH OHOH OHOH OHOH OHOH C O OHOH Glucose Fructose

26. H H H H H H H H H H O C C CC O OH HO OH CH 2 OH C OH O Structural formula Abbreviated structure Simplified structure 6 5 4 3 2 1

27.  Functional Groups  Functional groups are groups of atoms that give a molecule its characteristic properties.  Carbohydrates have 2 functional groups =  Hydroxyl -OH  Carbonyl -COH

28. Here you see 2 monosaccharides coming together to form a disaccharide. What type of reaction is this? _______________________________ Dehydration synthesis or condensation reaction

29.  Polymers =  Dissaccharide (two) Common examples are: Sucrose - sugar Maltose – grains (beer) Lactose - milk Lactose

31.  Polysaccharide (many) Common examples are: Starch - potato Cellulose – plant cell walls Glycogen - animals

32. Starch granules in potato tuber cells Glycogen granules in muscle tissue Cellulose fibrils in a plant cell wall Glucose monomer Cellulose molecules STARCH GLYCOGEN CELLULOSE O O O O OOO O OOO O O O O O O O O O O O O O O O O O O O O O OO OOOOO O O OO O OO O OH

33. -+-+

36. Remove Water Condensation Reaction / Dehydration Synthesis Monomer Polymer Add Water Hydrolysis Reaction

37.  Why does our body (and all living things) need this molecule?  Stores ENERGY  Insulation & Protection  Make up cell membranes (provide boundaries)  Where do we get this molecule?  Dairy products, Meat, Oil

38. Triglyceride

39.  Monomers  Glycerol  Fatty Acids Saturated Fatty Acids All Single Bonds Found in animals Solid at room temperature Unsaturated Fatty Acids At least 1 double or triple bond Found in plants Liquid at room temperature Animation

40.  To convert an oil into a solid at room temp.  Add hydrogens  Decreases the number of double bonds

41.  Functional Groups =  Hydroxyl  Carboxyl

42. Here you see 2 glycerol combining with a fatty acid in a dehydration reaction. This happens 3 times to create a triglyceride. animation

43.  Polymers =  Are very diverse BUT they are all hydrophobic  Examples; Triglyceride Steroids Wax Phospholipids

44. HO CH 3 H3CH3C A steroid – cholesterol. A molecule that is needed for cell membrane stability. Excess cholesterol due to consumption of fatty foods can lead to health problems like atherosclerosis (clogging of the arteries)

45.  Synthetic variants of male hormone – testosterone  Anabolism – building of substances by the body  Mimics testosterone which builds muscle tissue Overdosing – leads to serious side effects - depression, liver damage, shrunken testicles, breast development

48.  Drop each food sample onto a paper bag. Hold up to the light, it will turn translucent if lipids are present.  Sudan red is lipid soluble. The sudan red will stain the lipid layer. Solid red.

49. - +

50.  Why does our body (and all living things) need this molecule? o Make up our structure (actin in muscles, hemoglobin and antibodies in blood, etc)

52. Rate of reaction Temperature (  C) 020406080100 Enzyme AEnzyme B Speed up chemical reactions (enzymes)

53.  Where do we get this molecule? Dairy products, Meat, Beans, Nuts

54.  Monomers  Amino Acids There are only 20 different amino acids

56.  Functional Groups =  Amino – NH 2  Carboxyl - COOH

58. Fig. 3.14, p. 42 tyrosine (tyr)lysine (lys)glutamate (glu)glycine (gly) UNCHARGED, POLAR AMINO ACID POSITIVELY CHARGED, POLAR AMINO ACID NEGATIVELY CHARGED, POLAR AMINO ACID valine (val)phenylalanine (phe)methionine (met)proline (pro)

59. Here you see 2 amino acids combining in a dehydration reaction. Animation

60. Fig. 3.15, p. 43 newly forming polypeptide chain

61. One peptide group Fig. 3.17, p. 44

62.  Polymers = Polypeptides  Poly means many, peptide comes from the bonding

63. Fig. 3.16, p. 43 disulfide bridges

64.  The shape of a protein determines its function.  Shape depends on the interaction of the R groups of each amino acid forming weak H bonds.  Because H bonds are weak they can be broken by exposure to extreme pH or temperature, and certain chemicals like salt.  When a proteins shape is altered and therefore it stops functioning correctly we say it has been denatured.

65. Levels of Protein Structure Primary structure Gly Thr Gly Glu SerLys Cys Pro LeuMet Val Lys Val Leu Asp AlaVal Arg Gly Ser Pro Ala Ile Asn Val Ala Val His Val Secondary structure C N O C C N H O C C H Hydrogen bond O C N H C C O N H O C C N H C N O C C N H O C C N H C O C H N H C O H C R H N Alpha helix Amino acids C N H C C H H O N R C C O N H O C C N H C C O N H O C C N H C O C N H O C C N H C O O C C N H C C O N H C C O N H C C O N H C C O N H C C O N H C C O N H C C O H N C Pleated sheet Tertiary structure Polypeptide (single subunit of transthyretin) Quaternary structure Transthyretin, with four identical Polypeptide subunits Phe Arg

66. c) Tertiary structure of one polypeptide chain. The 3 D shape created by interactions of R groups.

67.  A well known example is hemoglobin, which consists of 2 alpha and 2 beta chains, consisting of 141 and 146 amino acid residues respectively.

68. Fig. 3.18, p. 44 beta chain beta chain alpha chain heme group twists and coils in the polypeptide chain of a globin molecule alpha chain

69. Levels of Protein Structure Gly Thr Gly Glu SerLys Cys Pro LeuMet Val Lys Val Leu Asp AlaVal Arg Gly Ser Pro Ala Ile Asn Val Ala Val His Val Weak hydrogen and ionic bonds C N O C C N H O C C H Hydrogen bond O C N H C C O N H O C C N H C N O C C N H O C C N H C O C H N H C O H C R H N Alpha helix Amino acids C N H C C H H O N R C C O N H O C C N H C C O N H O C C N H C O C N H O C C N H C O O C C N H C C O N H C C O N H C C O N H C C O N H C C O N H C C O N H C C O H N C Pleated sheet Hydrogen, ionic, and disulfide bridges Polypeptide (single subunit of transthyretin) Not all reach this structure Transthyretin, with four identical Polypeptide subunits Phe Arg Covalent bonds - peptide

71.  Proteins are the keys to the mysteries of how our bodies function.  Research biologists explore the shapes of proteins and how they work  A huge area of protein chemistry is in the medical field  Antibodies to fight infections, disease, cancers  Proteins that do not function properly in human beings with disease

72.  http://www.ebi.ac.uk/pdbe- apps/quips?story=Sunhats http://www.ebi.ac.uk/pdbe- apps/quips?story=Sunhats  http://www.ebi.ac.uk/pdbe- apps/quips?story=XmasFactor

75.  Why does our body (and all living things) need this molecule?  Stores and expresses the directions for how to make proteins  AKA: the blueprint for life  Where do we get this molecule?  We inherit this molecule from our parents and find it in all of the foods we eat.

77.  Monomers  Nucleotides 3 parts

78. Sugar-phosphate backbone T G C T A Nucleotide

79. C TA GC C G T A CG A T A G C A T AT T A Base pair T

80. … OH+HH Short polymerMonomer H2OH2O H2OH2O Dehydration Hydrolysis … Longer polymer H

81.  Cellular energy - ATP

82.  Polymers =  DNA Deoxyribose Sugar Bases: A, C, G, and T  RNA Ribose Sugar Bases: A, C, G, and U