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Chapter 5 The Structure and Function of Macromolecules
The Molecules of Life ,[object Object],[object Object],[object Object]
Macromolecules ,[object Object],[object Object],Figure 5.1
Macromolecules ,[object Object],[object Object],[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object],[object Object]
The Synthesis and Breakdown of Polymers ,[object Object],(a) Dehydration reaction in the synthesis of a polymer HO H 1 2 3 HO HO H 1 2 3 4 H H 2 O Short polymer Unlinked monomer Longer polymer Dehydration removes a water molecule, forming a new bond Figure 5.2A
The Synthesis and Breakdown of Polymers ,[object Object],[object Object],(b) Hydrolysis of a polymer HO 1 2 3 H HO H 1 2 3 4 H 2 O H HO Hydrolysis adds a water molecule, breaking a bond Figure 5.2B
[object Object],[object Object]
Carbohydrates ,[object Object],[object Object]
Sugars ,[object Object],[object Object],[object Object],[object Object],[object Object]
[object Object],H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH HO  C  H H  C  OH H  C  OH H  C  OH H  C  OH HO  C  H HO  C  H H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH H  C  OH C  O C  O H  C  OH H  C  OH H  C  OH HO  C  H H  C  OH C  O H H H H H H H H H H H H H H C C C C O O O O Aldoses Glyceraldehyde Ribose Glucose Galactose Dihydroxyacetone Ribulose Ketoses Fructose Figure 5.3 Triose sugars (C 3 H 6 O 3 ) Pentose sugars (C 5 H 10 O 5 ) Hexose sugars (C 6 H 12 O 6 )
[object Object],[object Object],[object Object],H H  C  OH HO  C  H H  C  OH H  C  OH H  C O C H 1 2 3 4 5 6 H OH 4 C 6 CH 2 OH 6 CH 2 OH 5 C H OH C H OH H 2  C 1 C H O H OH 4 C 5 C 3  C H H OH OH H 2 C 1  C OH H CH 2 OH H H OH HO H OH OH H 5 3  2 4 (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. OH 3 O H O O 6 1 Figure 5.4
[object Object],[object Object],[object Object]
Dehydration Synthesis (Condensation) Reactions & Hydrolysis Reactions ,[object Object],[object Object],[object Object]
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.  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. H 2 O CH 2 OH Glucose Fructose Sucrose H HO H H OH H OH O H OH CH 2 OH H H O H HO H OH O H CH 2 OH CH 2 OH HO OH H CH 2 OH H OH H O H OH CH 2 OH H HO O H O 1 2 1–2 glycosidic linkage H H HO H H OH H OH O H OH CH 2 OH H O H H OH H OH O H OH CH 2 OH H H 2 O H HO OH H CH 2 OH H OH H O H OH H CH 2 OH H OH H O H OH O 1 4 1–   4 glycosidic linkage Glucose Glucose Maltose OH H
Polysaccharides ,[object Object],[object Object],[object Object]
Storage Polysaccharides ,[object Object],[object Object],[object Object],Chloroplast Starch Amylose Amylopectin 1   m (a) Starch: a plant polysaccharide Figure 5.6
[object Object],[object Object],[object Object],Mitochondria Giycogen granules 0.5   m (b) Glycogen: an animal polysaccharide Glycogen Figure 5.6
Structural Polysaccharides ,[object Object],[object Object]
[object Object],(c) Cellulose: 1– 4 linkage of    glucose monomers H O O CH 2 OH H OH H H OH OH H H HO 4 C C C C C C H H H HO OH H OH OH OH H O CH 2 OH H H H OH OH H H HO 4 OH CH 2 OH O OH OH HO 4 1 O CH 2 OH O OH OH O CH 2 OH O OH OH CH 2 OH O OH OH O O CH 2 OH O OH OH HO 4 O 1 OH O OH OH O CH 2 OH O OH O OH O OH OH (a)    and    glucose ring structures (b) Starch: 1– 4 linkage of    glucose monomers 1    glucose    glucose CH 2 OH CH 2 OH 1 4 4 1 1 Figure 5.7 A–C
[object Object],Plant cells 0.5   m Cell walls Cellulose microfibrils  in a plant cell wall  Microfibril CH 2 OH CH 2 OH OH OH O O OH O CH 2 OH O O OH O CH 2 OH OH OH OH O O CH 2 OH O O OH CH 2 OH O O OH O O CH 2 OH OH CH 2 OH OH O OH OH OH OH O OH OH CH 2 OH CH 2 OH OH O OH CH 2 OH O O OH CH 2 OH OH ,[object Object],O O O O O O Parallel cellulose molecules are held together by hydrogen bonds between hydroxyl groups attached to carbon atoms 3 and 6. About 80 cellulose molecules associate to form a microfibril, the main architectural unit of the plant cell wall . A cellulose molecule is an unbranched   glucose polymer. OH OH O O OH Cellulose molecules
[object Object],[object Object],Figure 5.9
[object Object],[object Object],[object Object],(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.   O CH 2 OH OH H H OH 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.  OH Figure 5.10 A–C
Lipids ,[object Object],[object Object],[object Object],[object Object]
Fats ,[object Object],[object Object]
Fats ,[object Object],[object Object]
Fats ,[object Object]
“ Fatty” Acids ,[object Object]
[object Object],[object Object],[object Object],(a)  Saturated fat and fatty acid Stearic acid Figure 5.12
[object Object],[object Object],(b)  Unsaturated fat and fatty acid cis  double bond causes bending Oleic acid Figure 5.12
[object Object],[object Object],[object Object]
[object Object],[object Object],CH 2 O P O O O CH 2 CH CH 2 O O 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 + Figure 5.13  N(CH 3 ) 3
[object Object],Hydrophilic head  WATER WATER Hydrophobic tail  Figure 5.14
Steroids ,[object Object],HO CH 3 CH 3 H 3 C CH 3 CH 3 Figure 5.15
Steroids ,[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object],HO CH 3 CH 3 H 3 C CH 3 CH 3 Figure 5.15
Proteins ,[object Object],[object Object],[object Object]
[object Object]
[object Object],[object Object],Substrate (sucrose)  Enzyme  (sucrase)  Glucose OH H  O H 2 O Fructose 3   Substrate is converted to products.  1  Active site is available for a molecule of substrate, the reactant on which the enzyme acts. Substrate binds to enzyme.  2 2 4   Products are released. Figure 5.16
Polypeptides ,[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],[object Object]
Twenty Amino Acids ,[object Object],O O – H H 3 N + C C O O – H CH 3 H 3 N + C H C O O – CH 3 CH 3 CH 3 C C O O – H H 3 N + CH CH 3 CH 2 C H H 3 N + CH 3 CH 3 CH 2 CH C H H 3 N + C CH 3 CH 2 CH 2 C H 3 N + H C O O – CH 2 C H 3 N + H C O O – CH 2 NH H C O O – H 3 N + C CH 2 H 2 C H 2 N C CH 2 H C Nonpolar Glycine (Gly) Alanine (Ala) Valine (Val) Leucine (Leu) Isoleucine (Ile) Methionine (Met) Phenylalanine (Phe) C O O – Tryptophan (Trp) Proline (Pro) H 3 C Figure 5.17 S O  O –
O – OH CH 2 C C H H 3 N + O O – H 3 N + OH CH 3 CH C C H O – O SH CH 2 C H H 3 N + C O O – H 3 N + C C CH 2 OH H H H H 3 N + NH 2 CH 2 O C C C O O – NH 2 O C CH 2 CH 2 C C H 3 N + O O – O Polar Electrically charged  – O O C CH 2 C C H 3 N + H O O – O – O C CH 2 C C H 3 N + H O O – CH 2 CH 2 CH 2 CH 2 NH 3 + CH 2 C C H 3 N + H O O – NH 2 C NH 2 + CH 2 CH 2 CH 2 C C H 3 N + H O O – CH 2 NH + NH CH 2 C C H 3 N + H O O – Serine (Ser) Threonine (Thr) Cysteine  (Cys) Tyrosine (Tyr) Asparagine (Asn) Glutamine (Gln) Acidic Basic Aspartic acid  (Asp) Glutamic acid  (Glu) Lysine (Lys) Arginine (Arg) Histidine (His)
Amino Acid Polymers ,[object Object],[object Object]
Protein Conformation and Function ,[object Object]
Four Levels of Protein Structure ,[object Object],[object Object],Figure 5.20 – Amino acid subunits + H 3 N Amino end o Carboxyl end o c Gly Pro Thr Gly Thr Gly Glu Seu Lys Cys Pro Leu Met Val Lys Val Leu Asp Ala Val Arg Gly Ser Pro Ala Gly lle Ser Pro Phe His Glu His Ala Glu Val Val Phe Thr Ala Asn Asp Ser Gly Pro Arg Arg Tyr Thr lle Ala Ala Leu Leu Ser Pro Tyr Ser Tyr Ser Thr Thr Ala Val Val Thr Asn Pro Lys Glu Thr Lys Ser Tyr Trp Lys Ala Leu Glu Lle Asp
[object Object],[object Object],[object Object],O C    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 H H Figure 5.20
[object Object],[object Object],[object Object],CH 2 CH O H O C HO CH 2 CH 2 NH 3 + C - O CH 2 O CH 2 S S CH 2 CH CH 3 CH 3 H 3 C H 3 C Hydrophobic  interactions and  van der Waals interactions  Polypeptide backbone Hyrdogen bond Ionic bond CH 2 Disulfide bridge
[object Object],[object Object],Polypeptide chain Collagen    Chains    Chains Hemoglobin Iron Heme
Review of Protein Structure Primary  Secondary  Tertiary  Quaternary  + H 3 N Amino end Amino acid subunits  helix
Sickle-Cell Disease: A Simple Change in  Primary Structure ,[object Object],[object Object]
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 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    subunit 1 2 3 4 5 6 7 3 4 5 6 7 2 1 Normal hemoglobin Sickle-cell hemoglobin . . . . . . Figure 5.21 Exposed hydrophobic region Val Thr His Leu Pro Glul Glu Val His Leu Thr Pro Val Glu
What Determines Protein Conformation? ,[object Object],[object Object]
[object Object],Denaturation Renaturation Denatured protein Normal protein Figure 5.22
The Protein-Folding Problem ,[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],Hollow cylinder Cap Chaperonin (fully assembled) Steps of Chaperonin Action:   An unfolded poly-   peptide enters the    cylinder from one end.  The cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide.  The cap comes off, and the properly folded protein is released. Correctly folded protein Polypeptide 2 1 3 Figure 5.23
[object Object],[object Object],Figure 5.24 X-ray diffraction pattern Photographic film Diffracted X-rays X-ray source X-ray  beam Crystal Nucleic acid Protein (a)  X-ray diffraction pattern (b)  3D computer model
Nucleic Acids ,[object Object],[object Object],[object Object],[object Object],[object Object]
The Roles of Nucleic Acids ,[object Object],[object Object],[object Object]
Deoxyribonucleic Acid ,[object Object],[object Object],[object Object]
DNA Functions ,[object Object],[object Object],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
The Structure of Nucleic Acids ,[object Object],[object Object],(a) Polynucleotide,  or nucleic acid 3’C 5’ end 5’C 3’C 5’C 3’ end OH Figure 5.26  O O O O
[object Object],[object Object],[object Object],Nitrogenous base Nucleoside O O O   O P CH 2 5’C 3’C Phosphate group Pentose sugar (b) Nucleotide Figure 5.26  O
Nucleotide Monomers ,[object Object],[object Object],(c) Nucleoside components Figure 5.26  CH CH Uracil (in RNA) U Ribose (in RNA) Nitrogenous bases  Pyrimidines C N N C O H NH 2 CH CH O C N H CH HN C O C CH 3 N HN C C H O O Cytosine C Thymine (in DNA) T N HC N C C N C CH N NH 2 O N HC N H H C C N NH C NH 2 Adenine A Guanine G Purines O HOCH 2 H H H OH H O HOCH 2 H H H OH H Pentose sugars Deoxyribose (in DNA) Ribose (in RNA) OH OH CH CH Uracil (in RNA) U 4’ 5 ” 3’ OH H 2’ 1’ 5 ” 4’ 3’ 2’ 1’
Nucleotide Polymers ,[object Object],[object Object]
Gene ,[object Object],[object Object]
The DNA Double Helix ,[object Object],[object Object],[object Object]
[object Object],[object Object],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 3’ end 5’ end New strands  3’ end 5’ end 5’ end Figure 5.27
A,T,C,G ,[object Object],[object Object]
DNA and Proteins as Tape Measures of Evolution ,[object Object],[object Object]
The Theme of Emergent Properties in the Chemistry of Life:  A Review ,[object Object],[object Object],[object Object],[object Object]

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05 macromolecules

  • 1. Chapter 5 The Structure and Function of Macromolecules
  • 2.
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  • 14.
  • 15. 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. 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. H 2 O CH 2 OH Glucose Fructose Sucrose H HO H H OH H OH O H OH CH 2 OH H H O H HO H OH O H CH 2 OH CH 2 OH HO OH H CH 2 OH H OH H O H OH CH 2 OH H HO O H O 1 2 1–2 glycosidic linkage H H HO H H OH H OH O H OH CH 2 OH H O H H OH H OH O H OH CH 2 OH H H 2 O H HO OH H CH 2 OH H OH H O H OH H CH 2 OH H OH H O H OH O 1 4 1– 4 glycosidic linkage Glucose Glucose Maltose OH H
  • 16.
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  • 43. O – OH CH 2 C C H H 3 N + O O – H 3 N + OH CH 3 CH C C H O – O SH CH 2 C H H 3 N + C O O – H 3 N + C C CH 2 OH H H H H 3 N + NH 2 CH 2 O C C C O O – NH 2 O C CH 2 CH 2 C C H 3 N + O O – O Polar Electrically charged – O O C CH 2 C C H 3 N + H O O – O – O C CH 2 C C H 3 N + H O O – CH 2 CH 2 CH 2 CH 2 NH 3 + CH 2 C C H 3 N + H O O – NH 2 C NH 2 + CH 2 CH 2 CH 2 C C H 3 N + H O O – CH 2 NH + NH CH 2 C C H 3 N + H O O – Serine (Ser) Threonine (Thr) Cysteine (Cys) Tyrosine (Tyr) Asparagine (Asn) Glutamine (Gln) Acidic Basic Aspartic acid (Asp) Glutamic acid (Glu) Lysine (Lys) Arginine (Arg) Histidine (His)
  • 44.
  • 45.
  • 46.
  • 47.
  • 48.
  • 49.
  • 50. Review of Protein Structure Primary Secondary Tertiary Quaternary + H 3 N Amino end Amino acid subunits  helix
  • 51.
  • 52. 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 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  subunit 1 2 3 4 5 6 7 3 4 5 6 7 2 1 Normal hemoglobin Sickle-cell hemoglobin . . . . . . Figure 5.21 Exposed hydrophobic region Val Thr His Leu Pro Glul Glu Val His Leu Thr Pro Val Glu
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