LS2 Lecture 2

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dante01
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149449
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LS2 Lecture 2
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2012-04-23 01:28:25
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Midterm
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  1. Biological Molecules
    • 1. Proteins
    • 2. Carbohydrates
    • 3. Nucleic acids
    • 4. Lipids
  2. Proteins: Individual units
    • 1. Amino acids
    • -20 different types
  3. Carbohydrates: Individual units
    • 1. Glucose
    • 2. Fructose
    • 3. Galactose
  4. Nucleic Acids: Individual units
    • 1. Nucleotides
    • -5 different types
  5. Lipids: Individual units
    • 1. Fatty acids
    • 2. Glycerols

    -Not big enough to be a macromolecule
  6. Condensation reactions
    1. chemical process by which 2 molecules are joined together to make a larger, more complex, molecule, with the loss of water.
  7. Hydrolysis
    A large molecule is split into smaller sections by breaking a bond, addition of water
  8. Most diverse and abundant molecule
    Proteins
  9. Essential Amino Acids
    • 1. Methionine
    • 2. Tryptophan
    • 3. Leucine
    • 4. Phenylalanine
    • 5. Threonine
    • 6. Valine
    • 7. Isoleucine
    • 8. Lysine
    • 9. Tyrosine
  10. 4 levels of protein structure
    • 1. Primary
    • 2. Secondary
    • 3. Tertiary
    • 4. Quaternary
  11. Primary Structure
    • -Sequence of amino acids
    • -condensation reactions
    • -peptide bonds
  12. Secondary structure
    • -Local motifs found in a protein
    • -Ex. Beta sheets, Alpha Helix
    • -Stabalized by the hydrogen bonds that form between different amino acids(carboxyl and amino group)
  13. Tertiary Structure
    • - 3D conformation of protein caused by interactions between between the R-groups of two polypeptide chains
    • -can be denatured by high heat or pH changes
    • -hydrophobic interaction
    • -hydrogen bonds
    • -ionic
  14. Quaternary Structure
    • -Multisubunit proteins
    • -each subunit has its own primary, secondary, and tertiary structure
    • - Results from the interaction of 2+ polypeptide chains
    • -Ex. Hemoglobin
  15. What is crucial to the functioning of some proteins? (Why we need them?)
    • 1. Shape
    • - Enzymes need certain surface shapes in order to bind substrates correctly
    • -Carrier proteins in the cell surface allow substances to enter the cell
    • - Chemical signaling, hormones bind to proteins on the cell surface membrane
  16. Functions of Proteins
    • 1. Structural support
    • 2. Protection: Help protect cell/tissues, form barriers
    • 3. Transport: Ionic transport
    • 4. Catalysis: Enzymes
    • 5. Defense: Antibodies are proteins
    • 6. regulation: Internal/External metabolic functions
  17. Polypeptide chain
    single, unbranched chain of amino acids
  18. Can proteins become non-functional?
    • - Yes because of loss of shape
    • -denatured
    • - temperature (98.6+), changes in pH
    • -Heat can permenately destroy protein
  19. Carbohydrate function
    • 1. Energy storage
    • 2. Structural components
  20. 4 major categories of carbohydrates
    • 1. Monosaccharides: glucose, fructose, galactose
    • 2. Disaccharides (2)
    • 3. Oligosaccharides (3-20)
    • 4. Polysaccharides (>20)
  21. Protein linkages
    • 1. Peptide bonds
    • - carboxyl group reacts with the amino group
  22. Carbohydrate linkages
    • 1. Glycosidic linkages
    • -covalent bond
  23. Lipid linkages
    • 1. Ester linkage
    • - carboxyl group of a fatty acid reacts with the hydroxyl group of triglycerol
  24. Nucleic acid linkage
    • 1. Phosphodiester bond
    • -covalent bond
    • - a phosphate group and two 5-carbon ring carbohydrates over two ester bonds
  25. Carbohydrate Polymers
    • -Polymers of glucose
    • 1. Starch: plant source
    • -can digest
    • -alpaglycosidic
    • 2. Glycogen: animal source
    • -found in livers and muscles
    • -highly branched
    • 3. Cellulose
    • -beta glycosidic
    • -can't digest
    • -cows can digest
  26. Types of starch
    • 1. Amylose
    • -straight chains of glucose units.
    • 2. Amylopectin
    • -branched
  27. Structural components
    • 1. Celluose
    • -plants
    • 2. Chitin
    • -exoskeleton of arthopods
  28. Chitin: chemically modified sugar
    1. Chemically modified by addinga nitrogen group
  29. Nucleic acids
    1. Polymers that ae specialized for storage and transmission of information
  30. Types of Nucleic acids
    • 1. DNA
    • 2. RNA
  31. Nucleotide structure
    • 1. Phosphate group
    • 2. Sugar
    • 3. Base
  32. Bases in Nucleotides
    • 1. Purines: Fused double ring structure
    • -A= Adenine
    • -G= Guanine
    • 2. Pyrimidines: Single ring structure
    • -C= Cystsine
    • -T= Thymine (only in DNA)
    • -U= Uracil (only in RNA)
  33. Ribose vs Deoxyribose
    Ribose has extra oxygen
  34. What does DNA do?
    1. Encodes hereditary information and transfers information to RNA molecules
  35. What does RNA do?
    1. Decodes to specify the sequence of amino acids in proteins
  36. Ribonucleotide ATP
    1. acts as energy transducer in many biochemical reactions
  37. Ribonucleotide GTP
    1. Powers protein synthesis
  38. cAMP(cyclic AMP)
    • 1. Special ribonucleotide
    • 2. Essential for hormone action and transfer of information by the nervous system
  39. How is the double helix stabalized in DNA?
    1. Hydrogen bonding

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