Organic Chemistry Review
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Organic Chemistry Review

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Review of Basic Organic Chemistry for Mid-term

Review of Basic Organic Chemistry for Mid-term

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Organic Chemistry Review Organic Chemistry Review Presentation Transcript

  • AIM: What do you need to know about organic chemistry? ORGANIC CHEMISTRY: Study of Substances containing Carbon; the Chemistry of Life!
  • ORGANIC CHEMISTRY
    • All the Major Chemicals in Living things Contain Carbon.
    • The major organic chemicals are:
      • Carbohydrates
      • Lipids
      • Nucleic Acids
      • Proteins
  • Polymers
    • Monomers Joined Together
    • Condensation reaction
    • Joins ): Monomers together
    • Hydrolysis: Breaks Monomers Apart
  • Carbohydrates
    • Carbohydrates are sugars and
    • Identify sugars by their ending in –ose.
    • Metabolism is the break down of food into sugar for energy.
    • Basics sugars are called monosaccharides and are made of a single monomer of carbon, hydrogen and oxygen in a 1:2:1 ratio.
    • Linked sugars are polysaccharides and are found in starches and cellulose.
  • Carbohydrates, I
    • Monosaccharides
    • √ CH2O formula
    • √ Used for cellular respiration;
  • Carbohydrates, II
    • Disaccharides
    • √ 2 Monosaccharides, Joined by condensation reaction
    • Sucrose (table sugar) √ most common disaccharide
  • Carbohydrates, III
    • Polysaccharides Storage of energy:
    • Starch~ glucose monomers
    • Animals: glycogen
    • Polysaccharides Structural: Cellulose~ most abundant organic compound;
  • Lipids
    • glycerol and fatty acid
    • Fats, phospholipids, steroids
    • Hydrophobic; H bonds in water exclude fats
    • 3 Fatty Acids to 1 Glycerol
    • Saturated vs. unsaturated fats; single vs. double bonds
  • Lipids, II
  • Phospholipids
    • 2 fatty acids instead of 3 (phosphate group)
    • ‘ Tails’ hydrophobic; ‘heads’ hydrophilic
    • Bilayer (double layer); cell membranes
  • Proteins
    • Importance: instrumental in nearly everything organisms do; 50% dry weight of cells
    • Monomer: amino acids (there are 20) ~ carboxyl (-COOH) group, amino group (NH 2 ), H atom, variable group (R)….
    • Three-dimensional shape (conformation)
    • Polypeptides (dehydration reaction): peptide bonds join amino acids together
  • Carbohydrates (and beyond …)
    • Glucose is the preferred energy source for the brain. Brain function drops off sharply if glucose is in short supply.
    • The breakdown of glucose for energy can be traced all the way through glycolysis, Kreb’s cycle and electron transport chain.
  • Lipids
    • Lipids include fats, waxes, and steroids.
    • Lipids are non-polar and do not dissolve in water.
    • Lipids store energy and are the basis for steroid hormone synthesis.
    • Phosphoplipids make up all cell membranes.
  • Lipids (and beyond …)
    • Phospholipids make up all cell membranes and play a large role in determining what gets in and out of the cell.
    • Hydrophilic and hydrophobic regions give phosopholipids their unique properties.
  • Proteins
    • Proteins are the cell’s molecular machinery.
    • Most catalysts are made of protein.
    • Proteins are linked chains of amino acids.
    • Proteins are synthesized by the ribosome from a code made of RNA.
  • Proteins (and beyond …)
    • Proteins gain their function from the way they fold.
    • Proteins act as catalysts (ENZYMES) by lowering activation energy.
    • Hemoglobin transports oxygen to all tissues and is made of 4 dimers.
    • Many proteins use minerals such as calcium or iron to aid in their function.
  • Nucleic Acids
    • Nucleic Acids are polymers consisting of many nucleotides monomers that serve as a blueprint for proteins.
    • There are two types of nucleic acids: Deoxyribonucleic acid (DNA) and Ribonucleic Acids (RNA).
    • DNA gains its function from its structure, the double helix.
  • Nucleic Acids
    • The helical backbone is made up of sugar and phosphates.
    • Each pair (in DNA) is made of one of the four nitrogenous bases: adenine, guanine, cytosine and thymine.
    • In order to maintain the integrity of the genome, each base can only pair with one other base through hydrogen bonding.
  • Enzymes
    • Enzymes are proteins that catalyze biochemical reactions by lowering the activation energy of reactions that would normally happen anyway.
    • Identify enzymes by the suffix –ase: helicase (splits DNA), lactase (breaks down lactose), polymerase (inhibits HIV).
  • Enzymes
    • This reaction normally happens (black), but is catalyzed by the enzyme (red). Free energy change ( Δ G) is constant, but lowers activation energy (E A ).
  • Enzymes
    • Enzymes bind substrates (enzyme reactant) into active sites ( pocket or groove on enzyme).
    • While the enzyme and the substrate are joined, the enzyme catalyzes the reaction and converts the substrate to the product(s).
  • Enzymes
    • The most classic example an enzymatic reaction is the hydrolysis of sucrose (table sugar) into glucose and fructose.
  • Enzymes
    • Another look…
  • Amino Acids
    • Amino acids are the building blocks of proteins.
    • Only twenty amino acids account for the amazing variety of proteins.
    • Amino acids are linked by peptide bonds.
    • Each amino acid has a carboxyl end and an amino end