Biochemistry

1. Biochemistry

2. Learning Objectives • Know how Monomers relate to Polymers • (Pre-AP) Know Hydrolysis & Dehydration synthesis are opposite reactions & what they make • Know what monomers make up the 4 major Polymers of biology • Know functions/examples of • Carbohydrates • Lipids/Fats • Nucleic Acids • Proteins • What Enzymes do and How they Work

3. Biochemistry: • Foods: • - STEAK • - BREAD • BEANS • PASTA • CHOCOLATE • LETTUCE • Essential Question: • Which food type is associated to which polymers: • Polymers • Carbohydrates • Lipids/Fats • Nucleic Acids • Proteins

4. Monomer- a small molecule that may become bonded to other monomers to form a polymer. (think of a single link in a long chain) Monomers & Polymerspg 45 Polymer- a large molecule composed of repeating structural units (monomers) that are typically held together with covalentbonds

5. Examples (proteins) (D.N.A.) (carbohydrates: starch, cellulose)

6. Polymerization Pg 45 • Polymers are formed by the process of polymerization • Macromolecules are very large polymers 2 ways to go: Creation or Destruction - Can make a polymer from bonding monomers to each other (like links in a chain) • Can break up a polymer into its thousands of monomer units (breaking up the links) THE MOST IMPORTATN INGREDIENT IN THE EITHER CASE IS H20

7. Building and Breaking Polymers • CONDENSATION Reaction: a chemical reaction where Monomers link to form polymers.   • Water is formed during the formation of the polymers • HYDROLYSIS : the BREAKDOWN of some complex polymers. Hydrolysis is the reversal of a condensation so water is used (consumed) in the reaction https://biology4isc.weebly.com/b-biomolecules.html

8. Condensation Reaction (Making the chain) (water created)

9. Condensation Reaction (Making the chain) (water created)

10. Hydrolysis (water consumed) (breaking down the chain)

11. Hydrolysis (water consumed)

12. The 4 Major Polymers of Biology • 1. Carbohydrates (C-H-O 1:2:1 ratio) • 2. Lipids (C-H-O) • 3. Nucleic Acid Chains (C-H-O-N-P) • 4. Proteins (C-H-O-N)…sometimes S

13. Saccharide = Sugars • MONOSACCHARIDES are simple sugars (1 ring) • Know Mono vs Di vs Poly • GLUCOSE • GALACTOSE = sugar found in milk • FRUCTOSE = fruit sugar • Chemical composition (C6 H12 O6)

14. Important Monosaccharides Glucose

15. DISACCHARIDES consist of two single sugars (monosaccharides) linked together by glycosidic linkage • (via condensation reaction) • Lactose = Milk sugar • Sucrose = Table sugar Pg 159

16. Carbohydrates

17. Carbohydrates Pg 159 • Polysaccharides made of long sugars (monosaccharides & disaccharides) linked together by glycosidic linkages(Condensation Reation)

18. Pg 159 Starch Glucose

19. Carbohydrate Examples: • Starch - Plants convert excess sugars into starches for long-term ENERGY storage (no FAT in plants) • Glycogen -Animals store glucose in the form of glycogen in the liver and muscles to be used as quick energy storage • Cellulose -a structural polysaccharide contained in the cell walls of plants (why plants can stand upright) • Chitin – a polysaccharide found in the cell walls of fungi and the exoskeletons of insects and arthropods

20. Pg 160 Lipids (a.k.a. fats) • Lipids are large, NONPOLAR organic molecules that do NOT dissolve in water • Monomers are: 3 Fatty acids & 1 Glycerol • Oils, fats, waxes, and steroids are lipid based • Lipid molecules use less OXYGEN than carbohydrates to store energy efficiently (great for insulation too) • Used a lot in the cell/plasma membrane

21. Pg 160 LipidsGlycerol + 3 fatty acids

22. Pg 160 2) Lipids • UNSATURATED FATS are a liquid at room temperature (OILS). • Has a Double bond on the carbon chain • SATURATED FATS are solid at room temperature • NO double bonds on the carbon chain

23. Lipids- Saturated or Unsaturated Fatty Acids Pg 160 Stearic acid Solid at room temp Saturated fatty acid Oleic acid Liquid at room temp Unsaturated fatty acid

24. Dehydration Synthesis Pg 160 LipidsGlycerol + 3 fatty acids

25. Pg 160 LipidsGlycerol + 3 fatty acids Both are unsaturated fats: can see the “kinks” in the fatty acid chains

26. Look at Pg 177 Phospholipids

27. Phospholipids – Make up the cell membrane This O–Atom has a negative charge This N–Atom has a positive charge

28. This N–Atom has a positive charge This O–Atom has a negative charge Pg 177 Phospholipids

29. Pg 177 Hydrophilic vs. Hydrophobic Hydrophilic = Water loving Hydrophobic = Water fearing

30. Phospholipids and water H O H Remember: water has POLAR covalent bonds

31. Functions of Fat 1. As a “Bank” of Energy for harsh times or when food is naturally scarce or when traveling very far (migration) or to fuel rapid growth Ex:

32. Functions of Fat 2. As Insulation against the cold or wet to keep body temperature stable Blubber (a special lipid) is common in deep aquatic mammals (helps them float too)

33. 3) Nucleic Acid Chains(DNA is polymer) Pg 163 Nucleotides (the monomer) consist of a 5-carbon sugar, a phosphate group, and a nitrogenous base.

34. RNA and DNA are made of nucleotides Pg 163 -Store and transmits genetic information Nucleotide

35. Nucleotides: Pg 163

36. Pg 161 4) ***Proteins*** (monomer are amino acids) • Proteins are long polymers made up of smaller monomers called AMINO ACIDS • Amino Acids differ ONLY in the type of R group they carry Amino acids composed of 3 parts • Amino Group • Carboxylic group • R-group (Makes 20 different amino acids)

37. Pg 161 Amino Acids • Amino acid structure: NH3 - C - COOH • Amino acids differ due to the R group • The structure of the R-group determines the chemical properties of the amino acid

38. Pg 161

39. 20 Amino Acids

40. Pg 161 Peptide Bonds – link amino acids

41. Proteins • **Each protein has a specific order of amino acids that allow it form a complex shape** • **Different shapes allow proteins to perform different functions** • Amino Acids can bond to each other, one at a time, forming a long chain called a POLYPEPTIDE. • Proteins are composed of one or more polypeptides.

42. Pg 162 Protein Conformation Primary Structure – sequence of amino acids Secondary structure – Folding and coiling due to H bond formation between carboxyl and amino groups of non-adjacent amino acid. R groups are NOT involved. Tertiary structure – disulfide bridges, ionic bonding, or h-bonding of R-groups Quaternary structure – 2+ amino acid chains R- group interactions, H bonds, ionic interactions

43. Pg 162 Primary Structure Again the Amino Acid order will determine how this protein folds on to it self (i.e. its final shape)

44. Pg 162 Secondary Structure

45. Pg 162 Tertiary Structure Parts of the protein begin to take shape thanks to chemical bonds like Hydrogen-bonds

46. Or simply Order  Shape  Function Pg 162 Quaternary Structure The final shape of the protein (quaternary structure) will determine what function the protein has in the cell. **REMEMBER** Amino Acid  Protein  Protein’s order shape Function

47. Pg 162 http://www.stolaf.edu/people/giannini/flashanimat/proteins/protein%20structure.swf Animation:

48. Or simply Order  Shape  Function Amino Acid  Protein  Protein’s order shape Function

49. Denaturing of Protein(screwing up it’s shape)

50. Denaturing of Protein • Proteins may lose their unqiue 3D shape (and not work) if there is… • Excessive heat • Changes in pH (acidic or basic) • Changes in pressure in a cell