Bio 214 lab

The flashcards below were created by user lacythecoolest on FreezingBlue Flashcards.

  1. ________ are th3e major macromolecular constituent of cells and are composed of one or more linear chains of ___________ linked together by peptide bonds in specific sequence
    • Proteins
    • Amino Acids
  2. All twenty amino acids share a common structure called the
    Conserved region
  3. What technique did we use to allow cellular structure to be seen with the light microscope?
  4. The diameter of the circle of light that you see when looking into a microscope is called?
    Field of view
  5. What stains the nucleus of a cell blue?
    methylene blue
  6. Name of the aquatic plant we used to observe cytoplasmic streaming
  7. Objective lenses powers
    • 4x
    • 10x
    • 40x
    • 100x
  8. magnification and um's per ocular unit of 4x
    • 40x
    • 25 um per oc
  9. magnification and um's per ocular unit of 10x
    • 100x
    • 10 um per oc
  10. magnification and um's per ocular unit of 40x
    • 400x
    • 2.5 um per oc
  11. another word for cytoplasmic streaming
  12. Volumes for the micropipettes
    • p20
    • p200
    • p1000
  13. what is the range of volume for a micropipette size p20?
    0.5-20 ul
  14. what is the range of volume for a micropipette size p200?
    20-200 ul
  15. what is the range of volume for a micropipette size p1000?
    100-1000 ul
  16. part of micropipette that allows you to adjust the volume that is measured
    volume adjustment dial
  17. part of micropipette that shows the volume that will be measure
    digital readout
  18. What is the ul's of p20, p200 and p100 if the digital readout is: 070
    • p20: 7.0ul
    • p200: 70ul
    • p1000: 700ul
  19. What is the second stopping point on the plunger for?
    Used for the complete discharging of solutions from the plastic tips
  20. How much is each micropipette?
  21. this measures how much light a sample absorbs
  22. What is the special sample holder called that's used for the spectrophotometers?
  23. conserved region
    • a-carbon
    • carboxyl group
    • amino group
    • hydrogen atom
  24. what is the R group attached too?
    a carbon
  25. analytical tool for distinguishing different biomolecules based on their chemical properties
  26. what is the filter paper composed of for chromatography
    • cellulose
    • *hydrophilic
  27. how is the solvent drawn up on chromatography paper.
    capillary action with hydrophobic organic solvent
  28. what is the rate related too for molecules moving up the chromatography paper?
    • affinity for the hydrophobic paper
    • if the molecule goes further its more hydrophilic
  29. What is the rate of movement of a biomolecule during paper chromatograph reported as?
    • Relative mobility(Rf)
    • distance/distance solvent moved
  30. rule of thumb for handling chromatography paper
    no bare hands
  31. Is a benzene ring hydrophobic or hydrophilic?
  32. How are polypeptides separated during SDS polyacrylamide Gell electrophoresis?
    by weight
  33. examples of housekeeping proteins
    • enzymes of glycolysis
    • proteins that package DNA
    • cytoskeletal proteins
  34. technique of separating charged particles in an electrical field
    * passing an electrical current through some medium
  35. which charged molecules move towards which charged electrodes on a SDS page?
    • positively charged particles to the negative cathode
    • negative to the anode
  36. what are the three factors that control the relative rate of movement of a particle in general electrophoresis?
    • mass
    • shape
    • charge
  37. SDS-page stands for?
    SDS polyacrylamide Gel Electrophoresis
  38. what molecules, in respect to mass, shape and charge will move faster for general electorphoresis?
    • smaller
    • less surface area
    • greater total charge
  39. How is SDS-page different from general electrophoresis?
    it separates polypeptides based only on molecular weight
  40. what is the gel-like medium through which the electric field is passed
  41. what does SDS stand for?
    sodium dodecyl sulfate
  42. 2 roles SDS plays in regards to the SDS page
    • denatures the protein
    • SDS molecules coat the protein giving it a uniform negative charge
  43. the distance migrated by a polypeptide is inversely proportional to
    the log of the polypeptides MW
  44. How is the standard curve generated for the SDS-page
    by using the stand proteins/housekeeping
  45. the 5 tissues we took from the mouse for the SDS page
    • liver
    • lung
    • muscle
    • kidney
    • heart
  46. what does the instructor use to stain the proteins for the SDS page lab?
    coomassie blue, for 1 hour
  47. what is lactose formed from?
    galactose and glucose
  48. what must be hydrolyzed for lactose to yield its component monosaccharides so they can be absorbed?
    beta=galactosidic bond
  49. what is the enzyme used for lactase and is the chemical analog of lactose
  50. The lactose product that is absorbing the light
  51. THe buffer for the lactose lab:
  52. Stopper for the lactose lab
  53. What does the DTT reducing agent do to proteins for the SDS page experiment?
    break disulfate bridge which is covalently bonded, then they can run as separate proteins
  54. How does glycerol help for the SDS page experiement?
    • reduces diffusion during loading
    • -its heavy & viscous
    • - goes through gel straight
  55. how does bromophenol blue help for the SDS page experiment?
    • indicates when to stop
    • shows where smallest molecules migrate
Card Set
Bio 214 lab
Lab practical #1
Show Answers