1. Chapter 5

2. Organic Compounds Hydrogen and other elements covalently bonded to carbon Examples important to life are: Carbohydrates Lipids Proteins Nucleic Acids

3. Carbon’s Bonding Behavior Outer shell of carbon has 4 electrons; can hold 8 Each carbon atom can form covalent bonds with up to four atoms It can bonds with itself or other atoms Ex. H-C=C-H

4. Bonding Arrangements Carbon atoms can form chains or rings Other atoms project from the carbon backbone

5. How do organic molecules react? With their Functional Groups Atoms or clusters of atoms that are covalently bonded to carbon backbone Give organic compounds their different properties

6. Examples of Functional Groups Hydroxyl group - OH in carbs and proteins Amino group- NH 3 + proteins (basic) Carboxyl group- COOH fats and proteins (acid) Phosphate group- PO 3 - nucleic acids (acidic) Sulfhydryl group- SH Between proteins

7. Types of Reactions Functional group transfer Electron transfer Rearrangement – one type of organic compound changed to another Ex. Carbs to fats Condensation/dehydration synthesis Cleavage - splits

8. Condensation

9. Condensation Reactions Form polymers from subunits Enzymes remove -OH from one molecule, H from another, form bond between two molecules Discarded atoms can join to form water

10. Hydrolysis

11. A type of cleavage reaction Breaks polymers into smaller units Enzymes split molecules into two or more parts An -OH group and an H atom derived from water are attached at exposed sites

12. Carbohydrates Monomers - Monosaccharides (simple sugars) Dimers - Oligosaccharides (short-chain carbohydrates) Polymers - Polysaccharides (complex carbohydrates)

13. Monomers = Monosaccharides Simplest carbohydrates Most are sweet tasting, water soluble Most have 5- or 6-carbon backbone Glucose (6 C)Fructose (6 C) Ribose (5 C)Deoxyribose (5 C) Functional group ____

14. Two Monosaccharides glucosefructose

15. Disaccharides Type of oligosaccharide Two monosaccharides covalently bonded Formed by condensation reaction + H 2 O glucosefructose sucrose

16. Polymers = Polysaccharides Straight or branched chains of many sugar monomers Most common are composed entirely of glucose Cellulose Starch (such as amylose) Glycogen

17. Cellulose and Starch

18. Glycogen Sugar storage form in animals Large stores in muscle and liver cells When blood sugar decreases, liver cells degrade glycogen, release glucose

19. Chitin Polysaccharide Nitrogen-containing groups attached to glucose monomers Structural material for hard parts of invertebrates, cell walls of many fungi

20. Lipids Most include fatty acids Fats Phospholipids Waxes Sterols and their derivatives have no fatty acids Tend to be insoluble in water Monomers are fatty acids and glycerol

21. Fats Fatty acid(s) attached to glycerol Triglycerides are most common

22. Fatty Acids Carboxyl group (-COOH) at one end Carbon backbone (up to 36 C atoms) Saturated - Single bonds between carbons Unsaturated - One or more double bonds

23. Three Fatty Acids stearic acidoleic acidlinolenic acid

24. Phospholipids Main components of cell membranes

25. Waxes Long-chain fatty acids linked to long chain alcohols or carbon rings Firm consistency, repel water Important in water-proofing

26. Sterols and Derivatives No fatty acids Rigid backbone of four fused-together carbon rings Cholesterol - most common type in animals

27. Amino Acid Structure amino group carboxyl group R group

28. Properties of Amino Acids Determined by the “R group” Amino acids may be: Non-polar Uncharged, polar Positively charged, polar Negatively charged, polar

29. Protein Synthesis Protein is a chain of amino acids linked by peptide bonds Peptide bond Type of covalent bond Links amino group of one amino acid with carboxyl group of next Forms through condensation reaction

30. Primary Structure Sequence of amino acids Unique for each protein Two linked amino acids = dipeptide Three or more = polypeptide Backbone of polypeptide has N atoms: -N-C-C-N-C-C-N-C-C-N- one peptide group

31. Protein Shapes Fibrous proteins Polypeptide chains arranged as strands or sheets Globular proteins Polypeptide chains folded into compact, rounded shapes

32. Primary Structure & Protein Shape Primary structure influences shape in two main ways: Allows hydrogen bonds to form between different amino acids along length of chain Puts R groups in positions that allow them to interact

33. Secondary Structure Hydrogen bonds form between different parts of polypeptide chain These bonds give rise to coiled or extended pattern Helix or pleated sheet

34. Examples of Secondary Structure

35. Tertiary Structure Folding as a result of interactions between R groups heme group coiled and twisted polypeptide chain of one globin molecule

36. Quaternary Structure Some proteins are made up of more than one polypeptide chain Hemoglobin

37. Enzyme Structure and Function Enzymes are catalytic molecules They speed the rate at which reactions approach equilibrium

38. Four Features of Enzymes 1) Enzymes do not make anything happen that could not happen on its own. They just make it happen much faster. 2) Reactions do not alter or use up enzyme molecules.

39. Four Features of Enzymes 3 ) The same enzyme usually works for both the forward and reverse reactions. 4) Each type of enzyme recognizes and binds to only certain substrates.

40. Activation Energy For a reaction to occur, an energy barrier must be surmounted Enzymes make the energy barrier smaller activation energy without enzyme activation energy with enzyme energy released by the reaction products starting substance

41. Factors Influencing Enzyme Activity Temperature pH Salt concentration Allosteric regulators Coenzymes and cofactors

42. Polypeptides with Attached Organic Compounds Lipoproteins Proteins combined with cholesterol, triglycerides, phospholipids Glycoproteins Proteins combined with oligosaccharides

43. Denaturation Disruption of three-dimensional shape Breakage of weak bonds Causes of denaturation: pH Temperature Destroying protein shape disrupts function

44. Nucleotide Structure Sugar Ribose or deoxyribose At least one phosphate group Base Nitrogen-containing Single or double ring structure

45. Nucleotide Functions Energy carriers Coenzymes Chemical messengers Building blocks for nucleic acids

46. ATP - A Nucleotide three phosphate groups sugar base

47. Nucleic Acids Composed of nucleotides Single- or double-stranded Sugar-phosphate backbone Adenine Cytosine

48. DNA Double-stranded Consists of four types of nucleotides A bound to T C bound to G

49. RNA Usually single strands Four types of nucleotides Unlike DNA, contains the base uracil in place of thymine Three types are key players in protein synthesis