Cell Bio Exam 1

  1. How long are proteins are proteins typically?
  2. How long is a cell typically?
  3. The cell looks like _______ on the inside
  4. What are cells made of? (4)
    • 1. Proteins
    • 2. Lipids
    • 3. Nucleic Acids
    • 4. small molecules
  5. In the double layer membrane, the are the lipid tails attracted to each other?
    No; hydrophobic tail is just repelled by water
  6. What happens in the nucleolus?
    rRNA production
  7. The Golgi Apparatus is responsible for ______
    • protein processing/ sorting
    • glycosylation
  8. What does the smooth ER do?
    produce and modify hydrophic molecules
  9. What does the rough ER do?
    ribosomes produce proteins that are soluble inside rough ER
  10. Mitochondria
    site of aerobic ATP production
  11. Lysosomes
    digestive; site of acidic hydrolases; breakdown of old cell parts and endo/phagocytosed materials
  12. peroxisomes
    perform oxidative breakdown of fatty acids and other hydrophobic molecules
  13. 4 Pillars of Cell Biology
    • 1. Biochem
    • 2. Genetics
    • 3. Microscopy
    • 4. Molecular Biology
  14. Biochemistry
    The study of structure, function, and interactions of biological macromolecules
  15. Microscopy
    • using electromagnetic radiation and lenses to visualize tiny objects
    • -Limit of resolution is related to wavelength of light
  16. Bright field microscopy
    works on live cells, but no gives information about contents
  17. Fluorescence microscopy
    makes use of fluorophores (absorb a high energy photon and emit a lower energy photon)
  18. Immunofluorescence (3 steps)
    • attach a fluorophore to a secondary antibody (ex GFP)
    • 1. Fix cell (kill)
    • 2. attach primary antibody
    • 3. attach secondary antibody to primary
  19. Electron microscopy
    • -high resolution
    • - inherently low contrast due to light makeup of cells
    • - Solution: fox cells and stain using heavy atoms (eg. uranylacetate)
  20. Genetics
    study of genes; relationship between genes and phenotypes
  21. Classical/Forward genetics
    identification of genes that are responsible for known phenotypes
  22. Reverse Genetics
    identification of phenotypes that are associated with known genes
  23. Molecular Biology
    use of recombinant DNA technology to manipulate and study genes and phenotypes
  24. EcoR1
    E. coli restriction 1- first restriction enzyme isolated. cuts DNA sequences in very precise predetermined locations
  25. differential centrifugation
    • -spin mixture at high G force for a few minutes
    • -separate pellet from supernatant
  26. SDS-PAGE
    • Gel electrophoresis
    • uses charges to pull DNA molecules apart. The smaller the molecule, the faster it will move in a given time and the further it will get down the gel. Based on Molecular Weight not radius
  27. Western Blot (steps)
    • 1. gel elctrophoresis
    • 2. transfer to introcellulose paper
    • 3. add primary antibody to find molecule of interest
    • 4. add secondary antibody to bind to primary. Chemi-lumocesence enzyme on antibody reacts chemically to produce a photon of light
  28. primary protein structure
    amino acid sequence
  29. secondary protein structure
    alpha helix, beta sheet; primary structure folding into a or b
  30. tertiary protein structure
    secondary elements come together to form a complex 3D strucure that is generally a functional protein
  31. quaternary protein structure
    complexes of proteins (eg. histones)
  32. chromatography
    separation of molecules based on size, hydrophobicity, charge, or specific biological interactions
  33. Ion exchange chromatography
    Separates proteins based on charge. Beads coated with DEAE (positive) are placed in a tube. the solution of proteins goes through the tubes, and the negatively charged proteins attach to the beads and the cation proteins are eluted. a salt  solution is used to elute the anions on the beads.
  34. Gel Filtration Chromatography
    • separates proteins based on size (Stokes Radius not molecular weight)
    • -smaller proteins get stuck for a little bit in the depressions in the beads, so they elute more slowly than the larger proteins which easily go around the beads
  35. Affinity Chromatography
    • exploits biochemical interactions
    • -molecules that bind to the protein of interest are covalently attached to the beads. The proteins not of interest are eluted first, then a salt change is used to elute the proteins of interest from the beads.
  36. Actin monomers have ____ interactions with each other
  37. actin and microtubles use _____ to produce work for movemetn
    nucleotide hydrolysis
  38. actin has a _____ end which is __ and a ______ end which is __

    actin grows faster at the ______ end
    barbed (+), Pointed (-)

  39. actin is only an ATPase when ___________
    it is in a filament (polymerized)
  40. treadmilling
    net addition at one end but net subtraction at the other
Card Set
Cell Bio Exam 1
exam 1