1. Most macromolecules are polymers, built from monomers Three of the classes of life’s organic molecules are polymers –Carbohydrates –Proteins –Nucleic acids

2. The Diversity of Polymers Each class of polymer –Is formed from a specific set of monomers –Each organism is unique based on the arrangement of monomers into polymers An immense variety of polymers can be built from a small set of monomers 1 2 3 HOH

3. Synthesis and Breakdown of Polymers Monomers form larger molecules by condensation reactions called dehydration reactions (a) Dehydration reaction in the synthesis of a polymer HOH 1 2 3 H 1 23 4 H H2OH2O Short polymer Unlinked monomer Longer polymer Dehydration removes a water molecule, forming a new bond Figure 5.2A

4. Polymers can disassemble by Hydrolysis (b) Hydrolysis of a polymer HO 1 2 3 H H 1 2 3 4 H2OH2O H Hydrolysis adds a water molecule, breaking a bond Figure 5.2B

5. Carbohydrates: Fuel and Building Material Carbohydrates –Include both sugars and their polymers Monosaccharide's –Are the simplest sugars –Can be used for fuel –Can be converted into other organic molecules –Can be combined into polymers

6. Starch: Major Storage Form of Glucose in Plants Chloroplast Starch Amylose Amylopectin 1  m (a) Starch: a plant polysaccharide Figure 5.6

7. Glycogen –Consists of glucose monomers –Is the major storage form of glucose in animals Mitochondria Glycogen granules 0.5  m (b) Glycogen: an animal polysaccharide Glycogen Figure 5.6

8. Cellulose: Structural Polysaccharide Is a polymer of glucose It has different glycosidic linkages than starch

9. Major component of the cell walls around plant cells

10. Cellulose is difficult to digest Cows have microbes in their stomachs to facilitate this process Fungi / Termites have Cellulobiase – See Biofuels lab later Figure 5.9

11. Chitin another important structural polysaccharide –Is found in the exoskeleton of arthropods –Can be used as surgical thread (a) The structure of the chitin monomer. O CH 2 O H OH H H H NH C CH 3 O H H (b) Chitin forms the exoskeleton of arthropods. This cicada is molting, shedding its old exoskeleton and emerging in adult form. (c) Chitin is used to make a strong and flexible surgical thread that decomposes after the wound or incision heals. OH Figure 5.10 A–C

12. Polypeptides –Are polymers of amino acids A protein –Consists of one or more polypeptides Amino acids –Are organic molecules possessing both carboxyl and amino groups –Differ in their properties due to differing side chains, called R groups

13. 20 different amino acids make up proteins O O–O– H H3N+H3N+ C C O O–O– H CH 3 H3N+H3N+ C H C O O–O– C C O O–O– H H3N+H3N+ CH CH3CH3 CH2CH2 C H H3N+H3N+ CH3CH3 CH3CH3 CH2CH2 CHCH C H H3N+H3N+ C CH3CH3 CH2CH2 CH2CH2 C H3N+H3N+ H C O O–O– CH2CH2 C H3N+H3N+ H C O O–O– CH 2 NH H C O O–O– H3N+H3N+ C CH 2 H2CH2C H2NH2N C CH2CH2 H C Nonpolar Glycine (Gly) Alanine (Ala) Valine (Val)Leucine (Leu)Isoleucine (Ile) Methionine (Met) Phenylalanine (Phe) C O O–O– Tryptophan (Trp) Proline (Pro) H3CH3C Figure 5.17 S O O–O–

15. Amino Acid Polymers Amino acids are linked by peptide bonds DESMOSOMES OH CH 2 C N H C H O HOH Peptide bond OH H H HH H H H H H H H H N N N N N SH Side chains SH OO OO O H2OH2O CH 2 C C C CCC C C C C Peptide bond Amino end (N-terminus) Backbone (a) Figure 5.18 (b) Carboxyl end (C-terminus)

16. Protein Conformation and Function A proteins specific conformation (shape) –Determines how it functions Two examples of how the shape of a protein is displayed (a) A ribbon model (b) A space-filling model Groove

17. Four Levels of Protein Structure Primary structure –Is the unique sequence of amino acids in a polypeptide

18. OC  helix  pleated sheet Amino acid subunits N C H C O C N H C O H R C N H C O H C R N H H R C O R C H N H C O H N C O R C H N H H C R C O C O C N H H R C C O N H H C R C O N H R C H C O N H H C R C O N H R C H C O N H H C R C O N H H C R N H O O C N C R C H O C H R N H O C R C H N H O C H C R N H C C N R H O C H C R N H O C R C H H C R N H C O C N H R C H C O N H C Secondary structure –Is the folding or coiling of the polypeptide into a repeating configuration –Includes the  helix and the  pleated sheet –Hydrogen bonding is what causes these shapes to form

19. Tertiary structure The overall three-dimensional shape of a polypeptide Results from; – interactions between R groups –hydrophilic and hydrophobic interactions, –van der Waals forces, –Ionic interactions –hydrogen bonding. Disulphide bridges (strong covalent) also form between cysteine residues.

20. Tertiary structure The overall three-dimensional shape of a polypeptide CH 2 CH OHOH O C HO CH 2 NH 3 + C -O-O CH 2 O SS CH CH 3 H3CH3C H3CH3C Hydrophobic interactions and van der Waals interactions Polypeptide backbone Hydrogen bond Ionic bond CH 2 Disulfide bridge

21. Quaternary structure the overall protein structure that results from combining two or more polypeptide subunits Held together by weak forces –hydrophilic and hydrophobic interactions, –van der Waals forces, –ionic interactions and hydrogen bonding –Allows for “induced fit”

22. Proteins have many structures, resulting in a wide range of functions

23. What Determines Protein Conformation? Protein shape –Depends on the physical and chemical conditions of the protein’s environment – ionic, pH, temperature conditions Denaturation –Is when a protein unravels and loses its native conformation –Any situation which impacts the bonding arrangement of the protein Denaturation Renaturation Denatured proteinNormal protein Figure 5.22

24. Chaperonins –Are protein molecules that assist in the proper folding of other proteins

25. X-ray crystallography –Is used to determine a protein’s three- dimensional structure X-ray diffraction pattern Photographic film Diffracted X-rays X-ray source X-ray beam Crystal Nucleic acidProtein (a) X-ray diffraction pattern (b) 3D computer model Figure 5.24

26. Sickle-Cell Disease: A Simple Change in Primary Structure Sickle-cell disease –Results from a single amino acid substitution in the protein hemoglobin –Valine is substituted for Glutamic Acid at position 6 –Results in abnormal alpha and beta chains –Causes Hemoglobin to crystallize and RBC to sickle –Significant health impact

27. Hemoglobin structure and sickle-cell disease Fibers of abnormal hemoglobin deform cell into sickle shape. Primary structure Secondary and tertiary structures Quaternary structure Function Red blood cell shape Hemoglobin A Molecules do not associate with one another, each carries oxygen. Normal cells are full of individual hemoglobin molecules, each carrying oxygen     10  m     Primary structure Secondary and tertiary structures Quaternary structure Function Red blood cell shape Hemoglobin S Molecules interact with one another to crystallize into a fiber, capacity to carry oxygen is greatly reduced.  subunit 12 3 4 567 34 567 21 Normal hemoglobin Sickle-cell hemoglobin... Figure 5.21 Exposed hydrophobic region ValThrHisLeuProGlulGluValHisLeu Thr Pro Val Glu

28. LIPIDS ARE A DIVERSE GROUP OF HYDROPHOBIC MOLECULES Lipids –Are the one class of large biological molecules that do not consist of polymers –Share the common trait of being hydrophobic –Divided into FAT’S and OIL’S based on physical nature at room temperature Fats – Solid Oils - Liquids

29. Fats and Oils –Are constructed from two types of smaller molecules, a single glycerol and usually three fatty acids –Called triglyceride (TG, triacylglycerol, TAG, or triacylglyceride) H H

30. Saturated fatty acids –Have the maximum number of hydrogen atoms possible –Have no double bonds (a) Saturated fat and fatty acid Stearic acid Figure 5.12

31. Unsaturated fatty acids –Have one or more double bonds (b) Unsaturated fat and fatty acid cis double bond causes bending Oleic acid Figure 5.12

32. Fatty acids –Vary in the length and number and locations of double bonds they contain –No double bonds – all saturated fats –Double bonds - unsaturated fats One double bond – monounsaturated fatty acis Two or more – poly unsaturated fat Omega 3 – first double bond at “third” carbon from rhs Omega 6 - first double bond at “sixth” carbon from rhs Most people unaware of the vast variety of fatty acids of all types and the fact that foods we use as sources of fat contain combinations of many different fats

33. Phospholipids –Have only two fatty acids –Have a phosphate group instead of a third fatty acid –Results in a molecule with a hydrophilic “head” and hydrophobic “tails”

34. Phospholipid structure CH 2 O P O O O CH CH 2 OO C O C O Phosphate Glycerol (a) Structural formula (b) Space-filling model Fatty acids (c) Phospholipid symbol Hydrophobic tails Hydrophilic head Hydrophobic tails – Hydrophilic head CH 2 Choline + N(CH 3 ) 3

35. The structure of phospholipids –Results in a bilayer arrangement found in cell membranes Hydrophilic head WATER Hydrophobic tail Figure 5.14

36. Summary of fats

37. All Diets are High Fat Diets 200 lb man 2500 calories day – maintenance 30% Fats – 750 calories 25% proteins – 625 calories 45% complex carbs - 1125 400lb man Needs 2500 calories day – for maintenance But eats 1500 calories only 30% Fats – 450 calories 25% proteins – 375 calories 45% complex carbs – 675 REST???? 1000 calories of fat So really – 1450 fat calories = 68% fat

38. Steroids –Are lipids characterized by a carbon skeleton consisting of four fused rings –One steroid, cholesterol –Is found in cell membranes –Is a precursor for some hormones HO CH 3 H3CH3C Figure 5.15

39. NUCLEIC ACIDS STORE AND TRANSMIT HEREDITARY INFORMATION Genes –Are the units of inheritance –Program the amino acid sequence of polypeptides –Are made of nucleic acids

40. The Roles of Nucleic Acids There are two types of nucleic acids –Deoxyribonucleic acid (DNA) –Ribonucleic acid (RNA) DNA –Stores information for the synthesis of specific proteins –Directs RNA synthesis –Directs protein synthesis through RNA 1 2 3 Synthesis of mRNA in the nucleus Movement of mRNA into cytoplasm via nuclear pore Synthesis of protein NUCLEUS CYTOPLASM DNA mRNA Ribosome Amino acids Polypeptide mRNA Figure 5.25

41. The Structure of Nucleic Acids Nucleic acids –Exist as polymers called polynucleotides (a) Polynucleotide, or nucleic acid 3’C3’C 5’ end 5’C5’C 3’C3’C 5’C5’C 3’ end OH Figure 5.26 O O O O

42. Each polynucleotide –Consists of monomers called nucleotides Nitrogenous base Nucleoside O O OO OO P CH 2 5’C5’C 3’C3’C Phosphate group Pentose sugar (b) Nucleotide Figure 5.26 O

43. Nucleotide monomers –Are made up of nucleosides and phosphate groups (c) Nucleoside components Figure 5.26

44. Nucleotide polymers – Are made up of nucleotides linked by the–OH group on the 3´ carbon of one nucleotide and the phosphate on the 5´ carbon on the next The sequence of bases along a nucleotide polymer –Is unique for each gene

45. The DNA Double Helix Cellular DNA molecules –Have two polynucleotides that spiral around an imaginary axis –Form a double helix The DNA double helix –Consists of two antiparallel nucleotide strands

46. 3’ end Sugar-phosphate backbone Base pair (joined by hydrogen bonding) Old strands Nucleotide about to be added to a new strand A 3’ end 5’ end New strands 3’ end 5’ end Figure 5.27

47. The nitrogenous bases in DNA –Form hydrogen bonds in a complementary fashion (A with T only, and C with G only)

48. DNA and Proteins as Tape Measures of Evolution Molecular comparisons –Help biologists sort out the evolutionary connections among species