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PLTW MI > Unit 4.1 Manufacturing Human Proteins > Flashcards

Unit 4.1 Manufacturing Human Proteins Flashcards

1
Q

4.1.1 All about Insulin

What is insulin?

A
  • location: in pancreas
  • regulates blood suagr levels by reducing glucose levels
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2
Q

4.1.1 All about Insulin

Timeline for Diabetes

A
  • 1940s: Insulin and penicillin were used to help with diabetes
  • The 1950s: urine testing for monitoring glucose
  • 1960s: dialysis was invented
  • 1970/80s: home glucose monitoring was introduced
  • The 1990s: technology is being developed for body attachments
  • Modern times: diabetes is much more manageable and regulated and monitored
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3
Q

4.1.1 All about Insulin

Glucagon

A
  • location: in pancreas
  • regulate blood sugar levels by increase it
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4
Q

4.1.1 All about Insulin

Where do the sources of insulin come from?

A
  • dogs
  • cats
  • pigs
  • bacteria
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5
Q

4.1.1 All about Insulin

What are some common symptoms of diabetes?

A

freqeunt urination, thirst, fatigue

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6
Q

4.1.2 Protein Factories

What are the steps to genetically engineer bacteria to make human proteins?

A
  1. locate, isolate, remove gene of interest
  2. transform the bacteria
  3. allow bacteria to multiply
  4. lyse the bacteria
  5. collect proteins from the becateria
  6. seperate/purify proteins in the bacteria
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7
Q

4.1.2 Protein Factories

What is the purpose of plasmids?

A
  • small rings of DNA found in bacteria cells
  • human/animal/plant DNA can be placed into bacteria via this structure
  • altering this to include the code for a protein of interest
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8
Q

4.1.2 Protein Factories

What is bacterial transformation?

A
  • the manipulation of inserting bacteria into plasmids so that they can multiply in the cell
  • to produce insulin, green fluorscent protein (GFP) will be used in this bacterial transformaiton
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9
Q

4.1.2 Protein Factories

How can DNA be manipulated?

A
  • plasmid is cut using restriction enzymes
  • gene of interest is placed and glued within the opening of the plasmid using DNA ligase
  • the recombinant plasmid is then inserted into a cell
  • protein of interets is made in cell; cells duplicate to make more protein
  • is self ligation or inversion occurs, then the protein will not be coded
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10
Q

4.1.2 Protein Factories

What are the important parts to a plasmid?

A
  1. GFP gene (green): allows bacterial cells to produce GFP
  2. AMP^r (red): allows bacteria to be resistant to the antibiotic ampicillin; allows bacteria to frow on plates w/ ampicillin
    bla gene: encodes antibiotic resistance
  3. T7 promoter (yellow): on/off switch for GFP expression
    IPTG allows RNA plymerase to access promoter to turn off GFP production
  4. ori (grey): where bacteria can initiate copying of the plasmid
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11
Q

4.1.2 Protein Factories

What is the transformation efficency equation

A

total # of cells grwoing on the plate / amount of dna spread on the plate (in ug)

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12
Q

4.1.2 Protein Factories

What are the steps to lyse the transformed DNA?

A

lyse: breakapart DNA into smaller parts
1. detergent reacts with cell membrane
2. detergent destroys cell membrane
3. intracellular compenents are released

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13
Q

4.1.2 Protein Factories

How are bacterial proteins collected?

A
  • they are collected by centrifuging the sample
  • cell debris collects at bottom
  • protins are in the supernatant
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14
Q

4.1.2 Protein Factories

How are the proteins isolated?

A
  • chromotography
  • column is filled w/ a substance that allows desired proteins to be isolated from the others
  • loaded sample is placed in between stationary & mobile phase
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15
Q

4.1.2 Protein Factories

What are the 4 protein structures?

A
  1. primary: chain of amino acids
  2. secondary: hydrogen bonding of peptide backbone
  3. tertiary: three dimensional folding
  4. quaternary: consisting of more than one amino acid chain
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16
Q

4.1.2 Protein Factories

What is the difference between hydrophobic and hydrophilic interactions?

A
  • hydrophobic: water fearing (r group in the core region)
  • hydrophilic: water loving (r group in outside of molecule)
17
Q

4.1.2 Protein Factories

How is the purity of proetin samples analyzed

A
  • via electrophoresis
  • via SDS-PAGE
  • SDS - detergent (make it 2d structure) that denatures protens & adds a (-) charge to them
  • PA - material used to make gel
  • GE - gel electrophoresis: separates substances based on molecular size (this is vertical; not horizontal)

PLTW MI (6 decks)

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