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The Structure and Function of Macromolecules

The Structure and Function of Macromolecules. Macromolecules - larger molecules made from smaller ones. 4 major classes of macromolecules: carbohydrates, lipids, proteins, and nucleic acids. 3 of these are polymers because they are made from individual building blocks called monomers.

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The Structure and Function of Macromolecules

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  1. The Structure and Function of Macromolecules

  2. Macromolecules - larger molecules made from smaller ones. • 4 major classes of macromolecules: carbohydrates, lipids, proteins, and nucleic acids. • 3 of these are polymers because they are made from individual building blocks called monomers.

  3. http://www.diabetes.org.nz/pics/carbohydrate_foods.jpg

  4. Monomers - joined together through condensation or dehydration reaction (form macromolecules) • Requires energy; uses covalent bonds (links together monomers) • Water produced.

  5. Water produced as by-product

  6. Hydrolysis breaks polymers into monomers. • Water added to polymer; breaks bonds, creates monomers (i.e. digestive process in animals)

  7. Carbohydrates • 1Carbohydrates - sugars (monomers) and polymers. • AMonosaccharides - simple sugars. • BDisaccharides - double sugars (monosaccharides linked together) • CPolysaccharides - polymers of monosaccharides. • Sugars named with –ose.

  8. Monosaccharides needed for cellular work. • Help to synthesize other macromolecules.

  9. Maltose - 2 glucose molecules. • Sucrose - 1 glucose, 1 fructose.

  10. Polysaccharides - energy storage. • Starch - energy storage polysaccharide for plants. • Cellulose – polysaccharide; plant cell walls. • Animals store energy as glycogen.

  11. Chitin - polysaccharide - makes up exoskeleton of arthropods (like crustaceans and our sowbugs!).

  12. Chitin is used in surgery

  13. Lipids • Lipids - no polymers (exception) • Lipids nonpolar (no affinity for water) • Fat made from glycerol and fatty acids.

  14. Saturated fatty acid - No carbon-carbon double bonds in carbohydrate chain. (hydrogen at every possible position) • Form bad fats - solid at room temperature (butter, lard)

  15. No double-double bonds

  16. unsaturated fatty acid - 1+ carbon-carbon double bonds. • Formed by removal of hydrogen atoms from carbon skeleton. • Form good fats - liquid at room temperature (oils)

  17. Purpose of fat - energy storage. • Gram of fat stores 2X as much energy as gram of polysaccharide. • Fat also cushions vital organs. • Layer of fat can also function as insulation.

  18. http://www.healthline.com/blogs/diet_nutrition/uploaded_images/fat-cat-712938.jpghttp://www.healthline.com/blogs/diet_nutrition/uploaded_images/fat-cat-712938.jpg

  19. MOST IMPORTANT LIPID IN BIOLOGY = Phospholipid • Phospholipids have 2 fatty acids attached to glycerol. • Fatty acid tails are hydrophobic, phosphate group and attachments form hydrophilic head.

  20. When phospholipids added to water, self-assemble with hydrophobic tails pointing toward center, hydrophilic heads on outside. • Phospholipids in cell form bilayer; major component of cell membrane.

  21. Hydrophilic Hydrophobic

  22. Other Lipids • Steroids - lipids with carbon skeleton consisting of 4 fused carbon rings. • Cholesterol - component in animal cell membranes and hormones.

  23. Cholesterol

  24. Proteins • Proteins - support, storage, transport, defenses, and enzymes. • Made in ribosomes in cell. • Proteins - amino acids linked together to form polymer. • 20 different amino acids that can be linked together to form thousands of different proteins.

  25. http://images.foodnetwork.com/webfood/images/gethealthy/nutritionalallstars/LeanProteins_header.jpghttp://images.foodnetwork.com/webfood/images/gethealthy/nutritionalallstars/LeanProteins_header.jpg

  26. Amino acids link - polypeptides - combine to form proteins. • Amino acids made of hydrogen atom, carboxyl group, amino group, variable R group (or side chain). • R group makes amino acids different from one another.

  27. Shape of protein determines function. • Shapes - 3 dimensional - determined by sequence of amino acids.

  28. Primary structure of protein - linear sequence of amino acids determined by genetics.

  29. Secondary structure - two shapes are usually formed: alpha coils or beta sheets.

  30. Tertiary structure determined by interactions among R groups.

  31. Quarternary structure - joining of 2+ polypeptide subunits. • Collagen and hemoglobin examples.

  32. Protein’s shape can change due to environment. • pH, temperature, or salinity (salt concentrations) change - protein can denature (starts to fall apart) • Some proteins can return to functional shape after denaturation, others cannot.

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