Special Properties of Water due to H-bonding .

1. Special Properties of Water due to H-bonding. • It’s the UNIVERSAL SOLVENT • COHESIVE: water molecules “stick together”. This creates what’s called surface tension on bodies of liquid water. • High SPECIFIC HEAT; This means it gains and loses heat S..L..O..W..L..Y.

2. 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

3. Types of Reactions Functional group transfer Electron transfer Rearrangement **Condensation **Cleavage

4. A Word About Chemical Reactions • They are either Exergonic (release energy) • or Endogonic (gain energy) • Most reactions in biological systems are Exergonic • Breaking bonds ; releases energy • Making Bonds: endergonic • ANABOLIC; TO BUILD • CATABOLIC: TO BREAK DOWN

5. 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

6. Condensation

7. Hydrolysis • 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

8. Hydrolysis

10. Where Does This Occur in Your Body? • Hydrolysis Begins in your month, happens in your stomach and in your small intestines. • Dehydration Synthesis This takes place in your cells where most of your molecules are made

11. Organic Compounds • Hydrogen and other elements covalently bonded to carbon • Carbohydrates • Lipids • Proteins • Nucleic Acids

12. Each of the macromolecules (organic compound) has building blocks. • Be Familiar with these

13. Macromolecules • Polymers of repeating subunits • Carbohydrates (Starches and sugars) • Composed of Carbon (C), hydrogen (H), and oxygen (O) • Ratio of: C H2 O This one • Disaccharides (Sucrose) Monosaccharides(Glucose • Polysacchatarides (Srch, cellulose, glycogen)

14. Macromolecules (cont’d) • Functions • Structural support and barriers • Cellulose • Chitin • Nutrient and energy storage • Starch – Plant cells • Glycogen – Animal cells

15. glucose fructose 2 Monosaccharides

18. From Green To Yellow.. How Does My Banana Get So Sweet??

19. Crackers contain starch, a polysaccharide Digestion , starts in the mouth. Saliva contains ptylin an amylase. Digests starch to sugar Let’s Salivate!

22. Lipids Atoms--C, H, O Polymers? Monomers? For Fats Only (See Below There are different forms of Lipids: 1.Phospholipids 2. Fats 3. Steroids 4. Eicosanoids

23. Lipids Atoms--C, H, O (Ratio of H: O >2:1) Monomers –We have one for fat! Glycerol + 3 Fatty acids Function Concentrated energy storage Insulation Protection

27. Steroids STEROIDS: These have 4 interlocking rings

28. Cholesterol Structure provides membrane stability Component of steroid hormones

30. Other Lipid Molecules Phospholipids Glycerol + 2 fatty acids + phosphate Major component of cell membrane

31. Phospholipids • Main components of cell membranes

32. Eicosanoids • These are lipids that are derived from 20 carbon fatty acids found in all cell membranes • The function as hormone-like chemical signals between cells. • Most important are the Protaglandins which play a role in the immune system, specifically in inflammation, blood clotting labor contraction and role of blood vessel diameter. .

33. Example of a Prostaglandin: A modified fatty acid w/ carbon atoms arranged in a ring

35. PROTEINS • Proteins are composed of many subunits called amino acids. • There are different levels of organization for protein structure as dictated by their arrangement and bonding.

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

37. Amino Acid Structure R-

38. Examples of Amino Acids

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

40. Protein Structure Primary– The actual amino acid sequence Secondary--pleated sheet or alpha helix produced by hydrogen bonds Tertiary--folding based on other covalent bonds..NOW a GLOB. Quaternary--2 or more polypeptide chains.AT LEAST 2 GLOBS.

41. Primary Structure • Sequence of amino acids: SO PRIMARY STUCTURE MEANS JUST THIS…the SEQUENCE……..IT IS: • 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 W/PEPTIDE BOND

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

43. Secondary Pleated sheet, α-helix based on hydrogen bonds between R groups Pleated sheet, α-helix based on hydrogen bonds between R groups Primary Primary structure based on amino acid sequence Primary structure based on amino acid sequence

44. Examples of Secondary Structure

45. Tertiary Structure Folding as a result of interactions between R groups

46. Tertiary structure based on covalent and hydrogen bonds Quaternary structure—2 or more protein molecules

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

48. What ARE some Properties of PROTEINS in living systems?

49. Proteins are EVERYWHERE! Basically, 2 types of proteins: Fibrous and Globular Fibrous: These are your STRUCTURAL PROTEINS. Examples: Keratin ( found in hair and nails), Collagen found in skin, cartilage. Globular: FUNCTIONAL PROTEINS: Variety of functions, depends on specific protein….

50. How Do Globular Proteins Function? Protein function requires each molecule to have a unique Shape….So let’s See What We mean by that…