Biology 172 Lecture 3

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clintave
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130497
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Biology 172 Lecture 3
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2012-01-25 18:08:40
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Biology 172 Exam Review Lecture
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Biology 172 Exam Review Lecture 3
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  1. Molecules with a preponderance of nonpolar covalent bonds cannot form _______ _____ from ________ ______ with water and is called __________
    • covalent bonds
    • hydrogen bonds
    • hydrophobic
  2. It takes a lot of energy to change the ________ of water
    Temperature
  3. Substances that give up protons during chemical reactions to increase the proton concentration in water are called _____
    acids
  4. Substances that lower the proton concentration during chemical reactions are called ________
    bases
  5. Chemical properties of water that support life
    • Cohesion (hydrogen bonds)
    • Moderation of temperature (high specific heat)
    • Solvent for polar compounds
  6. Most chemical reactions important for life take place in _________ _________
    aqueous solutions
  7. pH scale = -log[H+]
    • an acid increases [H+]
    • a base reduces [H+]
    • a buffer minimizes changes in [H+] and [OH-]
  8. In cells, naturally occurring molecules act as ________ to maintain ___________
    • buffers
    • homeostasis
  9. Functional groups _, _, _ dictate the types of reactions that organic molecules participate in
    • N
    • O
    • H
  10. Monomers:
    Proteins
    Carbohydrates
    Nucleic Acids
    • Amino Acids
    • Monosaccharides
    • Nucleotides
  11. Polymers:
    Proteins
    Carbohydrates
    Nucleic Acids
    • Polypeptides (Proteins)
    • Polysaccharides
    • Nucleic Acids
  12. Proteins jobs
    • enzymes/ catalysis
    • structure
    • transport
    • signaling
    • defense
  13. Carbohydrates
    • fuel
    • building material
  14. Nucleic Acids
    • nucleotides (energy and signaling)
    • DNA = genetic info
    • RNA = intermediary between DNA and protein
  15. Lipids
    • fuel storage
    • membranes
    • hormones
  16. In size and shape, proteins are the most diverse class of molecules know
  17. Proteins Composed of Amino Acids
    • 20 different types
    • each has a carboxyl group and amino group
    • differ in charge, polarity, and size, and 'R' group
  18. At pH ___ (in a cell) the amino and carboxyl groups are ______
    • 7.2
    • ionized
  19. The side chain R groups are nonpolar.
  20. Biological macromolecules (DNA, carbohydrates, proteins) are assembled into polymers by condensation reactions:
    Condensation reactions: monomer in, water out (dehydration)

  21. What is this type of reaction called?
    what type of bond is formed?
    R-groups in this polypeptide?
    • Dehydration (from condensation)
    • Covalent (polar) bond
    • Polar

  22. Linear sequence of amino acids linked by ______ _____
    Sequence is determined by _______ ________
    Amino acids linked by ________ ______
    • peptide bonds
    • genetic instructions
    • covalent bonds

  23. why are polypeptide chains flexible?
    • 9 amino acids
    • Because the groups on either side of each peptide bond can rotate about their single bonds

  24. Why is this important?
    Importance of primary structure
  25. 2. Protein Secondary Structure
    Interactions between atoms in backbone held together by hydrogen bonds
  26. Two main secondary structures
    • -alpha helixes
    • -beta sheets
    • Stable 3D structures that form through hydrogen bonding of the backbone amino and carbonyl groups
  27. Secondary Structure
    Hydrogen bonds form between _____ _______ of one amino acid and ________ on amino group of another animo acid
    • carbonyl oxygen
    • hydrogen
  28. Noncovalent bonds help _______ _____
    proteins fold
  29. Electrostatic Interactions
    attractive forces between oppositely charged molecules H bonding : attraction between electropositive hydrogen atom and 2 electron attracting atoms, usually O or N
  30. Folded conformation in aqueous solution
  31. Tertiary structure - overall 3-D shape of polypeptide. Held together by ....
    • interactions between atoms in R groups
    • -hydrophobic
    • -van der Waals
    • -hydrogen bonds
    • -ionic bonds
    • -disulfide bridges
  32. Quaternary structure
    • Shape of a complex of multiple polypeptide chains (subunits)
    • Held together by covalent, ionic, hydrogen, and/or hydrophobic interactions

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