MolBiol #3.1

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Биохимия (макромолекулы) …

Биохимия (макромолекулы)
Аминокислоты и белки
Жирные кислоты и липиды
Нуклеотиды и нуклеиновые кислоты
Домашнее задание 1

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  • 1. Биологические макромолекулы
    • Белки
    • Углеводы
    • Липиды
    • Нуклеиновые кислоты
  • 2. Organic Compounds
    • Molecules unique to living systems contain carbon and hence are organic compounds
    • They include:
      • Carbohydrates
      • Lipids
      • Proteins
      • Nucleic Acids
  • 3. Carbohydrates
    • Contain carbon, hydrogen, and oxygen
    • Their major function is to supply a source of cellular food
    • Examples:
      • Monosaccharides or simple sugars
    Figure 2.14a
  • 4. Carbohydrates
    • Disaccharides or double sugars
    Figure 2.14b PLAY Disaccharides
  • 5. Carbohydrates
    • Polysaccharides or polymers of simple sugars
    Figure 2.14c PLAY Polysaccharides
  • 6. Lipids
    • Contain C, H, and O, but the proportion of oxygen in lipids is less than in carbohydrates
    • Examples:
      • Neutral fats or triglycerides
      • Phospholipids
      • Steroids
      • Eicosanoids
    PLAY Fats
  • 7. Neutral Fats (Triglycerides)
    • Composed of three fatty acids bonded to a glycerol molecule
    Figure 2.15a
  • 8. Other Lipids
    • Phospholipids – modified triglycerides with two fatty acid groups and a phosphorus group
    Figure 2.15b
  • 9. Other Lipids
    • Steroids – flat molecules with four interlocking hydrocarbon rings
    • Eicosanoids – 20-carbon fatty acids found in cell membranes
    Figure 2.15c
  • 10. Representative Lipids Found in the Body
    • Neutral fats – found in subcutaneous tissue and around organs
    • Phospholipids – chief component of cell membranes
    • Steroids – cholesterol, bile salts, vitamin D, sex hormones, and adrenal cortical hormones
  • 11. Representative Lipids Found in the Body
    • Fat-soluble vitamins – vitamins A, E, and K
    • Eicosanoids – prostaglandins, leukotrienes, and thromboxanes
    • Lipoproteins – transport fatty acids and cholesterol in the bloodstream
  • 12. Amino Acids
    • Building blocks of protein, containing an amino group and a carboxyl group
    • Amino group NH 2
    • Carboxyl groups COOH
  • 13. Amino Acids Figure 2.16a–c
  • 14. Amino Acids Figure 2.16d, e
  • 15. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17
  • 16. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17 Amino acid Amino acid Dehydration synthesis Hydrolysis Dipeptide Peptide bond + N H H C R H O N H H C R C C H O H 2 O H 2 O N H H C R C H O N H C R C H O OH OH OH
  • 17. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17 Amino acid Amino acid + N H H C R H O N H H C R C C H O OH OH
  • 18. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17 Amino acid Amino acid Dehydration synthesis + N H H C R H O N H H C R C C H O H 2 O OH OH
  • 19. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17 Amino acid Amino acid Dehydration synthesis Dipeptide Peptide bond + N H H C R H O N H H C R C C H O H 2 O N H H C R C H O N H C R C H O OH OH OH
  • 20. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17 Dipeptide Peptide bond N H H C R C H O N H C R C H O OH
  • 21. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17 Hydrolysis Dipeptide Peptide bond H 2 O N H H C R C H O N H C R C H O OH
  • 22. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17 Amino acid Amino acid Hydrolysis Dipeptide Peptide bond + N H H C R H O N H H C R C C H O H 2 O N H H C R C H O N H C R C H O OH OH OH
  • 23. Protein
    • Macromolecules composed of combinations of 20 types of amino acids bound together with peptide bonds
    Figure 2.17 Amino acid Amino acid Dehydration synthesis Hydrolysis Dipeptide Peptide bond + N H H C R H O N H H C R C C H O H 2 O H 2 O N H H C R C H O N H C R C H O OH OH OH
  • 24. Structural Levels of Proteins
    • Primary – amino acid sequence
    • Secondary – alpha helices or beta pleated sheets
    PLAY Chemistry of Life : Proteins: Secondary Structure PLAY Chemistry of Life : Proteins: Primary Structure PLAY Chemistry of Life : Introduction to Protein Structure
  • 25. Structural Levels of Proteins
    • Tertiary – superimposed folding of secondary structures
    • Quaternary – polypeptide chains linked together in a specific manner
    PLAY Chemistry of Life : Proteins: Quaternary Structure PLAY Chemistry of Life : Proteins: Tertiary Structure
  • 26. Structural Levels of Proteins Figure 2.18a–c
  • 27. Structural Levels of Proteins Figure 2.18b,d,e
  • 28. Fibrous and Globular Proteins
    • Fibrous proteins
      • Extended and strand-like proteins
      • Examples: keratin, elastin, collagen, and certain contractile fibers
  • 29. Fibrous and Globular Proteins
    • Globular proteins
      • Compact, spherical proteins with tertiary and quaternary structures
      • Examples: antibodies, hormones, and enzymes
  • 30. Protein Denuaturation
    • Reversible unfolding of proteins due to drops in pH and/or increased temperature
    Figure 2.19a
  • 31. Protein Denuaturation
    • Irreversibly denatured proteins cannot refold and are formed by extreme pH or temperature changes
    Figure 2.19b
  • 32. Molecular Chaperones (Chaperonins)
    • Help other proteins to achieve their functional three-dimensional shape
    • Maintain folding integrity
    • Assist in translocation of proteins across membranes
    • Promote the breakdown of damaged or denatured proteins
  • 33. Characteristics of Enzymes
    • Most are globular proteins that act as biological catalysts
    • Holoenzymes consist of an apoenzyme (protein) and a cofactor (usually an ion)
    • Enzymes are chemically specific
  • 34. Characteristics of Enzymes
    • Frequently named for the type of reaction they catalyze
    • Enzyme names usually end in -ase
    • Lower activation energy
  • 35. Characteristics of Enzymes Figure 2.20
  • 36. Mechanism of Enzyme Action
    • Enzyme binds with substrate
    • Product is formed at a lower activation energy
    • Product is released
    PLAY How Enzymes Work
  • 37. Figure 2.21 Active site Amino acids Enzyme (E) Enzyme-substrate complex (E-S) Internal rearrangements leading to catalysis Dipeptide product (P) Free enzyme (E) Substrates (S) Peptide bond H 2 O +
  • 38. Figure 2.21 Active site Amino acids Enzyme (E) Enzyme-substrate complex (E-S) Substrates (S) H 2 O +
  • 39. Figure 2.21 Active site Amino acids Enzyme (E) Enzyme-substrate complex (E-S) Internal rearrangements leading to catalysis Substrates (S) H 2 O +
  • 40. Figure 2.21 Active site Amino acids Enzyme (E) Enzyme-substrate complex (E-S) Internal rearrangements leading to catalysis Dipeptide product (P) Free enzyme (E) Substrates (S) Peptide bond H 2 O +
  • 41. Nucleic Acids
    • Composed of carbon, oxygen, hydrogen, nitrogen, and phosphorus
    • Their structural unit, the nucleotide, is composed of N-containing base, a pentose sugar, and a phosphate group
  • 42. Nucleic Acids
    • Five nitrogen bases contribute to nucleotide structure – adenine (A), guanine (G), cytosine (C), thymine (T), and uracil (U)
    • Two major classes – DNA and RNA
  • 43. Deoxyribonucleic Acid (DNA)
    • Double-stranded helical molecule found in the nucleus of the cell
    • Replicates itself before the cell divides, ensuring genetic continuity
    • Provides instructions for protein synthesis
  • 44. Structure of DNA Figure 2.22a
  • 45. Structure of DNA Figure 2.22b
  • 46. Ribonucleic Acid (RNA)
    • Single-stranded molecule found in both the nucleus and the cytoplasm of a cell
    • Uses the nitrogenous base uracil instead of thymine
    • Three varieties of RNA: messenger RNA, transfer RNA, and ribosomal RNA
  • 47. Adenosine Triphosphate (ATP)
    • Source of immediately usable energy for the cell
    • Adenine-containing RNA nucleotide with three phosphate groups
  • 48. Adenosine Triphosphate (ATP) Figure 2.23
  • 49. Figure 2.24 Solute Solute transported Contracted smooth muscle cell Product made Relaxed smooth muscle cell Reactants Membrane protein P P i ATP P X X Y Y + (a) Transport work (b) Mechanical work (c) Chemical work P i P i + ADP
  • 50. Figure 2.24 Solute Membrane protein P ATP (a) Transport work
  • 51. Figure 2.24 Solute Solute transported Membrane protein P P i ATP (a) Transport work P i + ADP
  • 52. Figure 2.24 Relaxed smooth muscle cell ATP (b) Mechanical work
  • 53. Figure 2.24 Contracted smooth muscle cell Relaxed smooth muscle cell ATP (b) Mechanical work P i + ADP
  • 54. Figure 2.24 Reactants ATP P X Y + (c) Chemical work
  • 55. Figure 2.24 Product made Reactants ATP P X X Y Y + (c) Chemical work P i P i + ADP
  • 56. Figure 2.24 Solute Solute transported Contracted smooth muscle cell Product made Relaxed smooth muscle cell Reactants Membrane protein P P i ATP P X X Y Y + (a) Transport work (b) Mechanical work (c) Chemical work P i P i + ADP
  • 57.
    • МЕТАБОЛИЗМ
  • 58.
    • Catabolism provides the building blocks and energy for anabolism.
    Figure 5.1
  • 59.
    • A metabolic pathway is a sequence of enzymatically catalyzed chemical reactions in a cell.
    • Metabolic pathways are determined by enzymes.
    • Enzymes are encoded by genes.
    PLAY Animation: Metabolic Pathways (Overview)
  • 60. Oxidation-Reduction
    • Oxidation is the removal of electrons.
    • Reduction is the gain of electrons.
    • Redox reaction is an oxidation reaction paired with a reduction reaction.
    Figure 5.9
  • 61. Oxidation-Reduction
    • In biological systems, the electrons are often associated with hydrogen atoms. Biological oxidations are often dehydrogenations.
    Figure 5.10
  • 62. The Generation of ATP
    • ATP is generated by the phosphorylation of ADP.
  • 63. The Generation of ATP
    • Substrate-level phosphorylation is the transfer of a high-energy PO 4 – to ADP.
  • 64. The Generation of ATP
    • Energy released from the transfer of electrons (oxidation) of one compound to another (reduction) is used to generate ATP by chemiosmosis.
  • 65. The Generation of ATP
    • Light causes chlorophyll to give up electrons. Energy released from the transfer of electrons (oxidation) of chlorophyll through a system of carrier molecules is used to generate ATP.