1.1.3 separation techniques Flashcards

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1
Q

what can centrifuges separate

A

substances of different densities

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2
Q

where do the more dense components settle in a centrifuge separation

A

in the pellet

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3
Q

where do the less dense components settle in the centrifuge separation

A

supernatant

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4
Q

how can paper and thin later chromatography be used

A

separate different substances such as amino acids and sugars

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5
Q

what can be used for separating different substances such as amino acids and sugars

A

paper and thin layer chromatography

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6
Q

what does the speed that each solute travels along the chromatogram depend on

A

different solubility in the solvent used

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7
Q

how does affinity chromatography work

A
  • a solid matrix or gel column is created with specific molecules bound to the matrix or gel
  • soluble, target proteins in a mixture with a high affinity for these molecules become attached to them as the mixture passes down the column
  • other non target molecules with a weaker affinity are washed out
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8
Q

how does gel electrophoresis work

A

charged nanomolecules move through an electric field applied to a gel matrix

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9
Q

how do native gels separate proteins

A

by shape charge and size

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10
Q

why do native gels separate proteins by size shape and charge

A

they do not denature the molecule

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11
Q

how does SDS-PAGE separate proteins

A

by size alone

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12
Q

how does SDS-PAGE separate proteins by size alone

A

it gives all the molecules an equally negative charge and denatures them

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13
Q

how else can proteins be separated from a mixture

A

through using thier isoelectric points in electrophoresis

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14
Q

what is an isoelectric point

A

the ph at which a soluble protein has no net charge and will precipitate out of solution

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15
Q

what will precipitate if a solution is buffered to a specific pH

A

the proteins with an isoelectric point of that pH

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16
Q

how can soluble proteins be separated

A

using an electric field and a pH gradient.

17
Q

when does a protein stop migrating through the gel in electrophoresis

A

at its isoelectric point in the pH gradient because it has no net charge