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Chapter 5

Chapter 5. Macromolecule. Missing carbohydrates. Lipids. Hydrophobic Consist mostly of hydrocarbons Include waxes, fats, phospholipids and steroids Monomers are glycerol and fatty acids 1:2 CH ratio with very little O Bond by an ester linkage. fatty acid. glycerol.

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Chapter 5

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  1. Chapter 5 Macromolecule

  2. Missing carbohydrates

  3. Lipids • Hydrophobic • Consist mostly of hydrocarbons • Include waxes, fats, phospholipids and steroids • Monomers are glycerol and fatty acids • 1:2 CH ratio with very little O • Bond by an ester linkage

  4. fatty acid glycerol

  5. Stearic acid Figure 5.12 (a) Saturated fat and fatty acid • Saturated fats contain single bonded carbons which allow the chains to tightly pack together.

  6. Oleic acid cis double bond causes bending Figure 5.12 (b) Unsaturated fat and fatty acid • Unsaturated fats contain double bonds, causing the chain to kink. This prevents the chains from compacting.

  7. + 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

  8. WATER Hydrophilic head WATER Hydrophobic tail Figure 5.14

  9. H3C CH3 CH3 CH3 CH3 HO Figure 5.15 • Steroids have 4 fused carbon rings as part of their structure Steroid cholesterol

  10. Proteins • From the Greek word “proteios”; meaning “first place” • Composed of CHON • No specific ratio • Monomers are amino acids • Bonded by peptide bond

  11. Table 5.1

  12. Substrate binds to enzyme. 2 2 1 Active site is available for a molecule of substrate, the reactant on which the enzyme acts. Substrate (sucrose) Glucose Enzyme (sucrase) OH H2O Fructose H O 4 Products are released. 3 Substrate is converted to products. Figure 5.16 • Enzymes serve as catalysts fro chemical reactions

  13. Peptidebond OH SH CH2 CH2 CH2 H H H C C H C C N C OH H C OH N N DESMOSOMES H O H O H O (a) H2O OH DESMOSOMES DESMOSOMES Side chains SH OH Peptidebond CH2 CH2 CH2 H H H N OH C C C C C H C N N Backbone H H O O H O Amino end(N-terminus) Carboxyl end(C-terminus) Figure 5.18 (b)

  14. Late 1940’s and early 1950’s, Fredrick Sanger of Cambridge University in England, worked on the hormone insulin and was able to determine the primary sequence of amino acids through enzymatic hydrolysis and chromatography.

  15. Pro Thr Gly Gly Thr Amino acid subunits +H3NAmino end 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 – Thr o Pro Asn Carboxyl end Figure 5.20 • Primary structure of a protein is its unique sequence of amino acids

  16. H H H H O O O O O O O H H 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 C Amino acidsubunits C N N N C C C R O H N H N H N H N N H N H H  helix C C O C R H H C C C H R R R R H H C C C C C C O O O O H C R O C C O O C H N N H C C R R • Secondary structure of proteins consists of repeated folds and coils held together by hydrogen bonds between backbones

  17. 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 proteins result from the interaction between “R” groups.

  18. Polypeptidechain Collagen  Chains Iron Heme  Chains Hemoglobin • Quaternary structure is composed of one or more polypeptide chains aggregated into one functional molecule

  19. 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     Hemoglobin A Quaternary structure Quaternary structure Hemoglobin S     Function Molecules interact with one another tocrystallize into a fiber, capacity to carry oxygen is greatly reduced. Function Molecules donot associatewith oneanother, eachcarries oxygen. 10 m 10 m Red bloodcell shape Normal cells arefull of individualhemoglobinmolecules, eachcarrying oxygen Red bloodcell shape Figure 5.21

  20. Denaturation Normal protein Denatured protein Renaturation Figure 5.22

  21. Correctlyfoldedprotein Polypeptide Cap Hollowcylinder The cap attaches, causing the cylinder to change shape insuch a way that it creates a hydrophilic environment for the folding of the polypeptide. The cap comesoff, and the properlyfolded protein is released. Chaperonin(fully assembled) Steps of ChaperoninAction: An unfolded poly- peptide enters the cylinder from one end. 2 1 3 Figure 5.23 • Chaperonin proteins assist in the conformational folding of proteins in the cells by isolating the proteins from “bad influences”

  22. Nucleoside Nitrogenous base O 5’C O O CH2 P O O Phosphate group 3’C Pentose sugar Figure 5.26 (b) Nucleotide • Nucleic acids are composed of nucleotides containing nitrogenous bases adenine, cytosine, thymine, guanine and uracil.

  23. Pyrimidines Nitrogenous bases Pyrimidines NH2 O O C C CH3 C N CH HN C CH HN CH CH CH C C C CH CH N N O N O O H H H Cytosine C Uracil (in RNA) U Thymine (in DNA) T Uracil (in RNA) U Purines O NH2 C C N N C C NH N HC HC C CH C N N NH2 N N H H Adenine A Guanine G Pentose sugars 5” 5” OH OH HOCH2 HOCH2 O O H H H H 1’ 1’ 4’ 4’ H H H H 3’ 2’ 3’ 2’ H OH OH OH Deoxyribose (in DNA) Ribose (in RNA) Ribose (in RNA)

  24. 3’ end 5’ end 5’ end Sugar-phosphatebackbone 5’C O Base pair (joined byhydrogen bonding) 3’C Old strands O Nucleotideabout to be added to a new strand 3’ end O A 5’ end 5’C O 3’C Newstrands 3’ end 3’ end OH 3’ end 5’ end Figure 5.27 Figure 5.26 RNA DNA

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