1 / 70

Chapter 5

Chapter 5. The Structure and Function of Macromolecules. The Molecules of Life. Overview: Another level in the hierarchy of biological organization is reached when small organic molecules are joined together Atom ---> molecule ---  compound. Figure 5.1. Macromolecules.

borka
Télécharger la présentation

Chapter 5

An Image/Link below is provided (as is) to download presentation Download Policy: Content on the Website is provided to you AS IS for your information and personal use and may not be sold / licensed / shared on other websites without getting consent from its author. Content is provided to you AS IS for your information and personal use only. Download presentation by click this link. While downloading, if for some reason you are not able to download a presentation, the publisher may have deleted the file from their server. During download, if you can't get a presentation, the file might be deleted by the publisher.

E N D

Presentation Transcript

  1. Chapter 5 The Structure and Function of Macromolecules

  2. The Molecules of Life • Overview: • Another level in the hierarchy of biological organization is reached when small organic molecules are joined together • Atom ---> molecule --- compound

  3. Figure 5.1 Macromolecules • Are large molecules composed of smaller molecules • Are complex in their structures

  4. Macromolecules • Most macromolecules are polymers, built from monomers • Four classes of life’s organic molecules are polymers • Carbohydrates • Proteins • Nucleic acids • Lipids

  5. A polymer • Is a long molecule consisting of many similar building blocks called monomers • Specific monomers make up each macromolecule • E.g. amino acids are the monomers for proteins

  6. 1 HO H 3 2 H HO Unlinked monomer Short polymer Dehydration removes a watermolecule, forming a new bond H2O 1 2 3 4 HO H Longer polymer (a) Dehydration reaction in the synthesis of a polymer Figure 5.2A The Synthesis and Breakdown of Polymers • Monomers form larger molecules by condensation reactions called dehydration synthesis

  7. 1 3 HO 4 2 H Hydrolysis adds a watermolecule, breaking a bond H2O 1 2 H HO 3 H HO (b) Hydrolysis of a polymer Figure 5.2B The Synthesis and Breakdown of Polymers • Polymers can disassemble by • Hydrolysis (addition of water molecules)

  8. Although organisms share the same limited number of monomer types, 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

  9. Carbohydrates • Serve as fuel and building material • Include both sugars and their polymers (starch, cellulose, etc.)

  10. Sugars • Monosaccharides • Are the simplest sugars • Can be used for fuel • Can be converted into other organic molecules • Can be combined into polymers

  11. Triose sugars(C3H6O3) Pentose sugars(C5H10O5) Hexose sugars(C6H12O6) H H H H O O O O C C C C H C OH H C OH H C OH H C OH H C OH H C OH HO C H HO C H Aldoses H H C OH H C OH HO C H H C OH H C OH H C OH Glyceraldehyde H C OH H C OH H Ribose H H Glucose Galactose H H H H C OH H C OH H C OH C O C O C O HO C H H C OH H C OH Ketoses H C OH H C OH H Dihydroxyacetone H C OH H C OH H C OH H Ribulose H Figure 5.3 Fructose • Examples of monosaccharides

  12. O H 1 C 6CH2OH 6CH2OH 2 CH2OH H C OH 5C H 5C O O 6 3 H O H H H H H 5 HO C H HOH H HOH 4 4C 1 C 1C 4C 4 1 OH H H H C OH O HO OH 3 2 OH OH 5 OH 2 C C 3 C 2C 3 OH H C H OH 6 H H OH OH H C OH H (a) Linear and ring forms. Chemical equilibrium between the linear and ring structures greatly favors the formation of rings. To form the glucose ring, carbon 1 bonds to the oxygen attached to carbon 5. Figure 5.4 • Monosaccharides • May be linear • Can form rings

  13. Disaccharides • Consist of two monosaccharides • Are joined by a glycosidic linkage

  14. (a) Dehydration reaction in the synthesis of maltose. The bonding of two glucose units forms maltose. The glycosidic link joins the number 1 carbon of one glucose to the number 4 carbon of the second glucose. Joining the glucose monomers in a different way would result in a different disaccharide. CH2OH CH2OH CH2OH CH2OH O O O O H H H H H H H H 1–4glycosidiclinkage HOH HOH HOH HOH 4 1 H H H H OH OH O H OH HO HO OH O H H H H OH OH OH OH H2O Glucose Maltose Glucose CH2OH CH2OH CH2OH CH2OH O O O O 1–2glycosidiclinkage H H H H H HOH HOH H 2 1 H OH H HO H HO H Dehydration reaction in the synthesis of sucrose. Sucrose is a disaccharide formed from glucose and fructose.Notice that fructose,though a hexose like glucose, forms a five-sided ring. (b) HO H O O HO CH2OH CH2OH OH H OH H H H OH OH H2O Glucose Sucrose Fructose Figure 5.5

  15. Polysaccharides • Polysaccharides • Are polymers of sugars • Serve many roles in organisms

  16. Chloroplast Starch 1 m Amylose Amylopectin (a) Starch: a plant polysaccharide Figure 5.6 Storage Polysaccharides • Starch • Is a polymer consisting entirely of glucose monomers • Is the major storage form of glucose in plants

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

  18. Structural Polysaccharides • Cellulose • Is a polymer of glucose

  19. H O CH2OH C CH2OH OH OH H C H O O H H H H HO OH OH C H 4 4 1 H H HO OH HO OH H H C OH OH H OH H C H OH  glucose C  glucose H (a)  and  glucose ring structures CH2OH CH2OH CH2OH CH2OH O O O O OH OH OH OH 1 4 4 4 1 1 1 HO O O O O OH OH OH OH (b) Starch: 1– 4 linkage of  glucose monomers OH CH2OH OH CH2OH O O OH OH O O OH OH HO OH 4 O 1 O O CH2OH CH2OH OH OH (c) Cellulose: 1– 4 linkage of  glucose monomers Figure 5.7 A–C • Has different glycosidic linkages than starch

  20. About 80 cellulose molecules associate to form a microfibril, the main architectural unit of the plant cell wall. Cellulose microfibrils in a plant cell wall Microfibril Cell walls  0.5 m Plant cells OH OH CH2OH CH2OH O O O O OH OH OH OH O O O O O OH CH2OH OH CH2OH Cellulose molecules CH2OH OH CH2OH OH O O O O OH OH OH OH Parallel cellulose molecules are held together by hydrogen bonds between hydroxyl groups attached to carbon atoms 3 and 6. O O O O O OH CH2OH OH CH2OH CH2OH CH2OH OH OH O O O O OH OH OH OH O O O A cellulose molecule is an unbranched  glucose polymer. O O OH CH2OH OH CH2OH Figure 5.8 • Glucose monomer • Is a major component of the tough walls that enclose plant cells

  21. Figure 5.9 • Cellulose is difficult to digest • Cows have microbes in their stomachs to facilitate this process

  22. CH2OH O OH H H OH H H H NH O C CH3 OH (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. (a) The structure of the chitin monomer. Figure 5.10 A–C • Chitin, another important structural polysaccharide • Is found in the exoskeleton of arthropods • Can be used as surgical thread

  23. Lipids • 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

  24. Fats • Are constructed from two types of smaller molecules, a single glycerol and usually three fatty acids • Vary in the length and number and locations of double bonds they contain

  25. Fats • Are constructed from two types of smaller molecules, a single glycerol and usually three fatty acids • Vary in the length and number and locations of double bonds they contain

  26. Fats • Are constructed from two types of smaller molecules, a single glycerol and usually three fatty acids

  27. Fats • Vary in the length and number and locations of double bonds they contain

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

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

  30. Phospholipids • Have only two fatty acids • Have a phosphate group instead of a third fatty acid

  31. + CH2 Choline N(CH3)3 CH2 O Phosphate Hydrophilic head – P O O O CH2 CH CH2 Glycerol O O C O C O Fatty acids Hydrophilic head Hydrophobic tails Hydrophobic tails (c) Phospholipid symbol (b) Space-filling model Figure 5.13 (a) Structural formula • Phospholipid structure • Consists of a hydrophilic “head” and hydrophobic “tails”

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

  33. Steroids • Steroids • Are lipids characterized by a carbon skeleton consisting of four fused rings

  34. H3C CH3 CH3 CH3 CH3 HO Figure 5.15 • One steroid, cholesterol • Is found in cell membranes • Is a precursor for some hormones

  35. Proteins • Proteins have many structures, resulting in a wide range of functions • Proteins do most of the work in cells and act as enzymes • Proteins are made of monomers called amino acids

  36. Table 5.1 • An overview of protein functions

  37. Substrate binds to enzyme. 1 Active site is available for a molecule of substrate, the reactant on which the enzyme acts. 2 2 Substrate (sucrose) Glucose Enzyme (sucrase) OH H2O Fructose H O 4 Products are released. 3 Substrate is converted to products. Figure 5.16 • Enzymes • Are a type of protein that acts as a catalyst, speeding up chemical reactions

  38. Polypeptides • Polypeptides • Are polymers (chains) of amino acids • A protein • Consists of one or more polypeptides

  39. Amino acids • Are organic molecules possessing both carboxyl and amino groups • Differ in their properties due to differing side chains, called R groups

  40. CH3 CH3 CH3 CH CH2 CH3 CH3 H CH3 H3C CH3 CH2 CH O O O O O H3N+ H3N+ H3N+ H3N+ C H3N+ C C C C C C C C C O– O– O– O– O– H H H H H Valine (Val) Leucine (Leu) Isoleucine (Ile) Glycine (Gly) Alanine (Ala) Nonpolar CH3 CH2 S H2C CH2 O NH CH2 H2N C C CH2 CH2 O– CH2 O O O H H3N+ H3N+ C C C C H3N+ C C O– O– O– H H H Phenylalanine (Phe) Proline (Pro) Methionine (Met) Tryptophan (Trp) Figure 5.17 Twenty Amino Acids • 20 different amino acids make up proteins

  41. OH NH2 O C NH2 O C OH SH CH2 CH3 OH Polar CH2 CH CH2 CH2 CH2 CH2 O O O O O O H3N+ H3N+ H3N+ H3N+ H3N+ H3N+ C C C C C C C C C C C C O– O– O– O– O– O– H H H H H H Glutamine (Gln) Tyrosine (Tyr) Asparagine (Asn) Cysteine (Cys) Serine (Ser) Threonine (Thr) Basic Acidic NH3+ NH2 NH+ O– O –O O CH2 C NH2+ C C NH Electrically charged CH2 CH2 CH2 CH2 CH2 O O H3N+ H3N+ CH2 CH2 C CH2 C C C O O– H3N+ O– CH2 C CH2 C H O H H3N+ O– C C CH2 H O O– H3N+ C C H O– H Lysine (Lys) Histidine (His) Arginine (Arg) Glutamic acid (Glu) Aspartic acid (Asp)

  42. Amino Acid Polymers • Amino acids • Are linked by peptide bonds

  43. Protein Conformation and Function • A protein’s specific conformation (shape) determines how it functions

  44. Amino acid subunits +H3NAmino end Pro Thr Gly Gly Thr Gly Glu Seu Lys Cys Pro Leu Met Val Lys Val Leu Asp Ala Arg Val Gly Ser Pro Ala Glu Lle Asp Thr Lys Ser Tyr Trp Lys Ala Leu Gly lle Ser Pro Phe His Glu His Ala Glu Val Thr Phe Val Ala Asn lle Thr Asp Ala Tyr Arg Ser Ala Arg Pro Gly Leu Leu Ser Pro Tyr Ser Tyr Ser Thr Thr Ala o Val c Val Glu – Lys o Thr Pro Asn Carboxyl end Figure 5.20 Four Levels of Protein Structure • Primary structure • Is the unique sequence of amino acids in a polypeptide

  45. H H H H H H O O O O O O O H H H H H H R R R R R R R C C C C C C C C C C C C C N N N N N N N N N N N N N C C C C C C C C C C C C C C R R R R R R H H H H H H H O O O O O O O H H H H H H H  pleated sheet H O H H Amino acidsubunits C C N N N C C C R H O H H H H H H N N N N N N  helix C C O C H H H C C C R R R R R H H C C C C C C O O O O H C R O C C O H C O N N H C C H R H R Figure 5.20 • Secondary structure • Is the folding or coiling of the polypeptide into a repeating configuration • Includes the  helix and the  pleated sheet

  46. Hydrophobic interactions and van der Waalsinteractions CH CH2 CH2 H3C CH3 OH Polypeptidebackbone H3C CH3 Hyrdogenbond CH O HO C CH2 CH2 S S CH2 Disulfide bridge O -O C CH2 CH2 NH3+ Ionic bond • Tertiary structure • Is the overall three-dimensional shape of a polypeptide • Results from interactions between amino acids and R groups

  47. Polypeptidechain Collagen  Chains Iron Heme  Chains Hemoglobin • Quaternary structure • Is the overall protein structure that results from the aggregation of two or more polypeptide subunits

  48. +H3N Amino end Amino acid subunits helix Review of Protein Structure

  49. Sickle-Cell Disease: A Simple Change in Primary Structure • Sickle-cell disease • Results from a single amino acid substitution in the protein hemoglobin

  50. Normal hemoglobin Sickle-cell hemoglobin Primary structure Primary structure . . . . . . Exposed hydrophobic region Val His Leu Thr Pro Glul Glu Val His Leu Pro Glu Thr Val 5 6 7 3 4 5 6 7 1 2 1 2 3 4 Secondaryand tertiarystructures Secondaryand tertiarystructures  subunit  subunit     Quaternary structure Hemoglobin A Quaternary structure Hemoglobin S     Molecules interact with one another tocrystallize into a fiber, capacity to carry oxygen is greatly reduced. Function Molecules donot associatewith oneanother, eachcarries oxygen. Function 10 m 10 m Normal cells arefull of individualhemoglobinmolecules, eachcarrying oxygen Red bloodcell shape Red bloodcell shape Figure 5.21 Fibers of abnormalhemoglobin deform cell into sickle shape.

More Related