AP BIO Ch 5 ppt

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AP BIO Ch 5 ppt

  1. 1. The Structure & Function ofThe Structure & Function of MacromoleculesMacromolecules
  2. 2. Your Goal  Name the monomers of the 4 macromolecules  Explain how those monomers are joined into polymers  Describe the uses of each macromolecule in living things
  3. 3. MacromoleculesMacromolecules Macromolecules are giant molecules made up of many small organic molecules joined together This is analogous to links joined together to make a chain
  4. 4. Most Macromolecules areMost Macromolecules are PolymersPolymers Built fromBuilt from MonomersMonomers Pectin is an example of a polymer. It is made up of repeating units of pectic acid and pectinic acid. These acid rings, then, are the monomers that link together to form pectin. Polymer Each ring, or link, in the chain is a monomer
  5. 5. The Synthesis of PolymersThe Synthesis of Polymers In order to covalently bond, the 2 monomers lose –H & -OH atoms which combine to form water as a bi-product. Thus this reaction is known as dehydration synthesis The process is then repeated many times to synthesize a large polymer. Note: Some texts may refer to this as a condensation reaction
  6. 6. ……And the Breakdown ofAnd the Breakdown of PolymersPolymers The reverse reaction for a dehydration synthesis is hydrolysis. A water molecule is used to break, or lyse, the covalent bond between two monomers. When the bonds are broken, energy is released.
  7. 7. When one organism eats another, macromolecules are broken down & their monomers can be reused and/or rearranged to make new polymers with different functions.
  8. 8. Polymer DiversityPolymer Diversity Variations among organisms is primarily a result of molecular differences; namely in their DNA & protein Although there’s a HUGE variety of polymers, but only 40-50 monomers exist! **The variety results from the order of a sequence of monomers. As a simple example, 4 monomers can be ordered in several configurations to yield polymers that have different structures and functions. STOP POTS TOPS It’s sort of like letters of the alphabet; different arrangements of the same letters form different words with very different meanings
  9. 9. Quick Think with your food buddy  Draw a monomer and a polymer
  10. 10. Four BiologicalFour Biological MacromoleculesMacromolecules
  11. 11. Carbohydrates Serve asCarbohydrates Serve as Fuel & Building MaterialFuel & Building Material Carbohydrates are sugars & starches There are 3 levels of carbohydrate complexity: Monosaccharides Disaccharides Polysaccharides (Mono means 1, saccharide refers to a sugar) (Di = 2) (Poly = Many) Vocab. Tip: Most sugars end in the suffix –ose. Glucose,Maltose, Lactose, etc
  12. 12. Monosaccharides-simplest of the sugars; consist of 1 ring Examples: Glucose & Fructose Main fuel for cells cellular respiration; used for quick energy. Monosaccharides that are left unused become linked by dehydration synthesis to form disaccharides & polysaccharides. Basic molecular formula = CH2O where there are generally twice as many H as C or O. Example: glucose C6H12O6 Like other sugars, glucose forms rings in water
  13. 13. Disaccharides – Consist of two monosaccharides joined together Examples: Maltose, Lactose, Sucrose 2 glucose monomers bond to make maltose, which has different chemical characteristics than glucose Name of bond between C1 & C4 Glucose + Fructose = Sucrose
  14. 14. Polysaccharides- Polymers of 100s to 1,000s of monosaccharides linked together Storage polysaccharides: Polymer Name Monomer Location Function In Plants Starch Glucose Plastids of cells Store surplus glucose In Animals Glycogen Glucose Liver & muscle cells Fuel storage used when glucose is unavailable
  15. 15. Structural Polysaccharides-insoluble & hard to break down (e.g. dietary fiber): Example in plants = cellulose Long, straight chains of glucose that are H-bonded to each other at their hydroxyl groups = microfibrils that form cell wall Example in animals = chitin Monomer is glucose with 1 hydroxyl group replaced with an acetylamino group Polysaccharides
  16. 16. Quick Think with your best thing buddy  Draw a monosaccharide  Draw a polysaccharide  Give one biological use for these molecules
  17. 17. Lipids are a DiverseLipids are a Diverse GroupGroup of Hydrophobic Moleculesof Hydrophobic Molecules Lipids are macromolecules that ARE NOT polymers Hydro = water Phobic = fearing Lipids are mostly hydrocarbons and, therefore, are hydrophobic Three biologically important lipids: 1. Fats 2. Phospholipids 3. Steroids
  18. 18. FatsFats Each molecule is made of 1 glycerol & 3 fatty acids Bonds form by dehydration synthesis Carboxyl group = fatty “acid” Triacylglycerol (a.k.a.triglyceride)Saturated fat = no double bonds between C in fatty acid chain Unsaturated fat = 1 or more double bonds between C in fatty acid chain
  19. 19. FatsFats Function = Energy storage *1 gram of fat stores more than twice as much energy as 1g of carbohydrate! *The fat molecules in animals are stored in adipose cells -Adipose layers protect organs & insulate Adipose Cells (40X) Whale Blubber
  20. 20. PhospholipidsPhospholipids Made of 1 glycerol & only 2 fatty acidsCharged phosphate group makes the head hydrophilic In water, phospholipids arrange into a bilayer according to their hydrophobic & hydrophilic regions Slightly positive H in water attracts negative phosphate group in phospholipids
  21. 21. SteroidsSteroids Steroids have this 4-ringed basic structure attached to a functional group This functional group makes this molecule cholesterol. *Cholesterol is a major component of animal cell membranes *Many sex hormones are made from cholesterol
  22. 22. Quick Think with your super hero buddy  Why are fats NOT polymers?  Name one biological use for lipids.
  23. 23. Proteins Have Many Structures,Proteins Have Many Structures, Resulting in a Wide Range of FunctionsResulting in a Wide Range of Functions Some protein functions: Enzymatic proteins- catalyze rxns Structural proteins- support Storage Proteins- storage of amino acids Transport proteins- transport other molecules Hormonal proteins- regulate organism’s activities Receptor proteins- allow cells to respond to stimuli Contractile proteins- movement Defensive proteins- protection against disease Hair Protein in seeds Hemoglobin Found in muscle cells
  24. 24. PolypeptidesPolypeptides •A protein is 1 or more polypeptides folded & coiled into a specific shape •A polypeptide is a polymer of amino acids One amino acid monomer linked to a chain of others. All of the amino acids linked together form a polypeptide chain
  25. 25. Polypeptides:Polypeptides: Amino Acid MonomersAmino Acid Monomers R group R group Leucine Serine Carboxyl groupAmino group Variable side group Each of the 20 different amino acids has a different R group which gives it its unique characteristics
  26. 26. Polypeptides:Polypeptides: Amino Acid PolymersAmino Acid Polymers Peptide Bond R group R group R group R group Amino group Carboxyl group N-terminus C- terminus Amino Acid chains are held together by peptide bonds which are formed by a dehydration reaction The number, type, & sequence of amino acids determine the shape and function of the polypeptide
  27. 27. Note that both the C & N-terminus ionize in aqueous solutions
  28. 28. Protein ConformationProtein Conformation & Function& Function The function of a protein is an emergent property resulting from its unique shape Model of receptor protein Model of enzyme In each example, the protein’s ability to perform its function is dependant on the specific shape of the protein
  29. 29. Protein Conformation & Function:Protein Conformation & Function: Four Levels of Protein StructureFour Levels of Protein Structure Primary Structure: a protein’s unique, linear sequence of amino acids which is determined by genetic information
  30. 30. Protein Conformation & Function:Protein Conformation & Function: Four Levels of Protein StructureFour Levels of Protein Structure Secondary Structure: the result of H-bonding between partially negative oxygen & nitrogen of the polypeptide backbone and hydrogen on the backbone. Primary Structure α-helix structure: coiling that results from H-bonding between every 4th amino acid β-pleated sheet: polypeptide backbone folds on itself, forming H-bonds
  31. 31. Protein Conformation & Function:Protein Conformation & Function: Four Levels of Protein StructureFour Levels of Protein Structure Tertiary structure: the overall shape of the polypeptide resulting from interactions between R- groups of amino acids. Hydrophobic interactions contribute to tertiary structure: hydrophobic R- groups are organized so that they are in the center of the protein. Hydrophilic amino acid R- groups end up on the outer surface of the protein. Note disulfide bridge reinforces protein conformation
  32. 32. Protein Conformation & Function:Protein Conformation & Function: Four Levels of Protein StructureFour Levels of Protein Structure Quaternary structure: forms when two or more polypeptide chains aggregate to make one molecule
  33. 33. Protein Conformation & Function:Protein Conformation & Function: Four Levels of Protein StructureFour Levels of Protein Structure •A protein’s shape is sensitive to the surrounding environment Unfavorable temperature and pH changes can cause a protein to unravel and lose its shape. This is called denaturation
  34. 34. Quick Think with your love buddy <3  Draw and label the 4 levels of protein structure
  35. 35. Nucleic AcidsNucleic Acids Store & TransmitStore & Transmit Hereditary InformationHereditary Information •Nucleic acids store the instructions for building proteins •Two types: Deoxyribonucleic Acid (DNA) & Ribonucleic Acid (RNA) •The flow of genetic information: DNA RNA protein
  36. 36. Nucleic Acid StructureNucleic Acid Structure Nucleic acids are polymers of nucleotides. Each nucleotide has 3 parts: 5-carbon sugar, phosphate group, & a nitrogenous base
  37. 37. Nucleic Acid Structure:Nucleic Acid Structure: Nucleotide MonomersNucleotide Monomers Nucleotides can have 1 of 4 different nitrogenous bases: cytosine, thymine – uracil in RNA- (pyrimidines) or adenine, guanine (purines) Thymine (T) Cytosine (C) Adenine (A) Guanine (G) p u r i n e s p y r i m i d i n e s
  38. 38. Nucleic Acid Structure:Nucleic Acid Structure: Nucleotide PolymersNucleotide Polymers Bond occurs at -OH on 3’ C of one nucleotide and the phosphate group on the 5’ C of the other nucleotide Bond formed is called a phosphodiester bond This process creates a sugar- phosphate backbone with the nitrogenous bases sticking out
  39. 39. The DNA Double HelixThe DNA Double Helix The two strands of the double helix are antiparallel, running in the 5’ 3’ direction H-Bonds
  40. 40. DNA & Proteins as TapeDNA & Proteins as Tape Measures of EvolutionMeasures of Evolution The sequence of nucleotides in DNA and the sequence of amino acids in proteins can be used to determine evolutionary relationships…closely related species have fewer differences in their sequences. Millionsofyearsago Amino acid differences compared with human hemoglobin
  41. 41. Quick Think  What are the names of the bonds between: 1. Sugars in a polysaccharide 2. Amino acids in a protein 3. Nucleotides in a nucleic acid

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