Unit 4.1 Flashcards

1
Q

Why is protein purification required?

A

to study structure and function

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2
Q

What challenges come with purifying proteins?

A
  • the mixture of proteins in cells/tissue
  • diversity of proteins (such as size, charge, binding characteristics, and cellular location)
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3
Q

what determines a protein’s separation/purification parameters and assay?

A

It’s size, charge, binding characteristics and cellular location

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4
Q

What is the order of the protein purification workflow?

A
  1. identify source (blood, cell type, etc)
  2. fractionation/enrichment (by centrifugation or salt fractionation)
  3. Purification
  4. monitoring purification (gel electrophoresis)
  5. quantification (protein concentration or enzyme activity)
  6. analysis (structure and function)
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5
Q

how does gel electrophoresis work?

A

molecules are separated in electrical field through a porous field acting as a molecular sieve.

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6
Q

what medium is usually used?

A

Polyacrylamide (proteins) and sometimes Agarose for nucleic acids

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7
Q

What type of proteins is electrophoresis used for?

A

both native and denatured, but mostly denatured

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