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Biol101 chp5-pp-fall10-101011181834-phpapp02
- 1. BIOL 101 General Biology I Chapter 5 The Structure & Function of Large Biological Molecules Rob Swatski Associate Professor of Biology HACC – York Campus1
- 3. 3 Bonds with variety of elements Diverse sizes & shapes Carbon-based Many covalent bonds More insoluble in water Monomers Polymers Properties of Organic Molecules
- 6. Dehydration Short polymer Unlinked monomer Longer polymer HO HO HO H2O H HH 4321 1 2 3 6
- 7. 7 Hydrolysis
- 8. Hydrolysis HO HO HO H2O H H H321 1 2 3 4 8
- 9. 9 3 Major Groups of Carbohydrates Mono- saccharides Disaccharides Polysaccharides
- 10. 10 Carbohydrate Characteristics C-H2O Classify by location of carbonyl (C=O) Aldoses or Ketoses #C atoms in skeleton
- 14. (a) Linear and ring forms (b) Abbreviated ring structure 14
- 16. 1–2 glycosidic linkage 16 Dehydration reaction: Sucrose synthesis SucroseFructoseGlucose
- 17. Maltose 1–4 glycosidic linkage 17 Dehydration reaction: Maltose synthesis GlucoseGlucose
- 18. 18 Polysaccharides Largest carb Polymer: 100’s of mono’s Storage and structure Classified by its monomer & linkages Glycogen
- 21. 21 Structural Polysaccharides Cellulose Glucose polymer Plant cell walls Alpha () & beta () rings beta ()
- 23. 23 and Glucose Ring Structures Glucose Glucose
- 24. Starch: 1–4 linkage of glucose monomers (Alpha) = All same side 24
- 25. 25 Cellulose: 1–4 linkage of glucose monomers (Beta) = Both sides
- 26. 26
- 28. 28 Symbiosis
- 29. 29 Chitin
- 30. Chitin is used to make a strong and flexible surgical thread that decomposes after the wound or incision heals. 30
- 31. 31 Hydrocarbons C, H, O Hydrophobic Nonpolar covalent bonds No polymers Glycerol & 1-3 fatty acids Fats & oils Lipids – General Characteristics
- 33. Fatty acid Glycerol Dehydration synthesis of a fat Ester linkage Triglyceride 33
- 35. Fatty Acid Variation Length # and locations of double bonds Saturated fatty acids Unsaturated fatty acids 35
- 37. 37 Unaturated Fats Cis double covalent bond Liquid @ room temp Mostly plant & fish fats
- 38. 38
- 42. 42 Head Polar Hydrophilic Glycerol & phosphate Tails Nonpolar Hydrophobic 2 Fatty acids Phospholipid Structure
- 45. 45
- 47. 47 Steroids
- 48. 48
- 49. 49
- 50. 50 Proteins C, H, O, N Diverse shapes & sizes Polypeptides (polymers) Amino acids (monomers)
- 51. 51 Enzymatic Structural Storage Transport Hormonal Receptor Contractile & Motor Defensive Types of Proteins
- 52. 52 Structural support Storage Transport Communication Movement Immune defense Functions of Proteins
- 54. 60 m Collagen Connective tissue Structural proteins Function: Support Examples: Keratin is the protein of hair, horns, feathers, and other skin appendages. Insects and spiders use silk fibers to make their cocoons and webs, respectively. Collagen and elastin proteins provide a fibrous framework in animal connective tissues. 54
- 56. Signaling molecules Receptor protein Receptor proteins Function: Response of cell to chemical stimuli Example: Receptors built into the membrane of a nerve cell detect signaling molecules released by other nerve cells. 56
- 57. 57 Actin & Myosin: contractile proteins
- 58. Muscle tissue Actin Myosin 100 m Contractile and motor proteins Function: Movement Examples: Motor proteins are responsible for the undulations of cilia and flagella. Actin and myosin proteins are responsible for the contraction of muscles. 58
- 60. Defensive proteins Virus Antibodies Bacterium Function: Protection against disease Example: Antibodies inactivate and help destroy viruses and bacteria. 60
- 62. Enzymatic proteins Enzyme Example: Digestive enzymes catalyze the hydrolysis of bonds in food molecules. Function: Selective acceleration of chemical reactions 62
- 64. 64 Amino Acids Amino group - NH2 Carboxyl group - COOH R group
- 66. Side chain Glycine (Gly or G) Alanine (Ala or A) Valine (Val or V) Leucine (Leu or L) Isoleucine (Ile or I) Methionine (Met or M) Phenylalanine (Phe or F) Tryptophan (Trp or W) Proline (Pro or P) Nonpolar Amino Acids (hydrophobic) 66
- 67. Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y) Asparagine (Asn or N) Glutamine (Gln or Q) Polar Amino Acids (hydrophilic) 67
- 68. Acidic (negatively charged) Basic (positively charged) Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Arginine (Arg or R) Histidine (His or H) Electrically Charged Amino Acids (hydrophilic) 68
- 69. Peptide bond New peptide bond forming Side chains Back- bone Amino end (N-terminus) Peptide bond Carboxyl end (C-terminus) 69
- 70. 70 Functional Proteins Ribbon model of lysozyme Space-filling model of lysozyme Groove Groove
- 71. 71
- 72. Antibody protein Protein from flu virus 72
- 75. Primary structureAmino acids Amino end Carboxyl endPrimary structure of transthyretin 75
- 76. pleated sheet helix Secondary Structure 76
- 77. Hydrogen bond helix pleated sheet strand, shown as a flat arrow pointing toward the carboxyl end Hydrogen bond Secondary Structure 77
- 78. 78Silk = pleated sheet
- 79. 79 too freakin’ cute… …it has eyelashes for crying out loud!
- 81. Hydrogen bond Disulfide bridge Polypeptide backbone Ionic bond Hydrophobic interactions and van der Waals interactions 81
- 83. Collagen 83
- 84. 84 Collagen
- 85. Hemoglobin Heme Iron subunit subunit subunit subunit 85
- 86. 86 Sickle-Cell Disease Glutamic acid Valine (mutation)
- 87. No interaction between molecules Normal hemoglobin 7654321 GluVal His Leu Thr Pro Glu 87 Normal hemoglobin (top view)
- 88. Sickle-cell hemoglobin Sickle-cell hemoglobin 7654321 ValVal His Leu Thr Pro Glu Exposed hydrophobic region 88 Interaction between molecules = crystal fiber
- 89. Primary Structure Secondary and Tertiary Structures Quaternary Structure Function Red Blood Cell Shape subunit subunit Exposed hydrophobic region Molecules do not associate with one another; each carries oxygen. Molecules crystallize into a fiber; capacity to carry oxygen is reduced. Sickle-cell hemoglobin Normal hemoglobin 10 m 10 m Sickle-cellhemoglobinNormalhemoglobin 1 2 3 4 5 6 7 1 2 3 4 5 6 7 89
- 90. 90 Physical & Chemical Conditions Affect Protein Structure pH changes Salt concentration Temperature Denaturation
- 92. 92 Protein Folding in the Cell Chaperonin
- 93. 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. Polypeptide Correctly folded protein Steps of Chaperonin Action: An unfolded poly- peptide enters the cylinder from one end. The cap comes off, and the properly folded protein is released. 32 1 Steps of Chaperonin Action 93
- 96. 96
- 97. 97CoA Binding Site in Staphylococcus aureus
- 98. EXPERIMENT RESULTS X-ray source X-ray beam Diffracted X-rays Crystal Digital detector X-ray diffraction pattern RNA polymerase II RNA DNA 98
- 99. 99 Bioinformatics Predicts protein structure from AA sequence
- 100. 100
- 101. 101 C, H, O, N, P Polymer of nucleotides DNA and RNA Molecular biology Regulates cell activities Guides protein synthesis Nucleic Acids
- 102. 102 mRNA 1. Synthesis of mRNA in the nucleus DNA NUCLEUS mRNA CYTOPLASM 2. mRNA moves into cytoplasm via nuclear pore Ribosome Amino acidsPolypeptide 3. Synthesis of protein
- 104. 5' end 5'C 3'C 5'C 3'C 3' end Polynucleotide (Nucleic Acid) Nucleotide Nucleoside Nitrogenous base 3'C 5'C Phosphate group Sugar (pentose) 104
- 105. Ribose (in RNA)Deoxyribose (in DNA) Sugars of the Nucleotide 105
- 106. Nitrogenous Bases of the Nucleotide Purines Guanine (G)Adenine (A) Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA) Pyrimidines 106
- 107. 107
- 109. Sugar-phosphate backbones 3' end 3' end 3' end 3' end 5' end 5' end 5' end 5' end Base pair Old strands New strands 109
- 110. Sugar-phosphate backbones Hydrogen bonds Base pair joined by hydrogen bonding Base pair joined by hydrogen bonding (b) Transfer RNA(a) DNA 5 3 53 110