Lecture 3 - Proteins for crystallography Flashcards

1
Q

Directional and gene-fragmentation cloning can produce many constructs to be

A

screened for expression

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2
Q

Expression system speed (low to high)

A

Mammalian
Insect
Yeast
Bacteria

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3
Q

Expression system cost (low to high)

A

Bacteria
Yeast
Insect
Mammalian

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4
Q

Expression system typical yield (low to high)

A

Mammalian
Insect
Bacteria
Yeast

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5
Q

Expression system post-translational modification (low to high)

A

Bacteria
Yeast
Insect
Mammalian

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6
Q

Expression system FDA approval (low to high)

A

Insect
Yeast
Bacteria
Mammalian

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7
Q

An affinity tag is typically for

A

purification

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8
Q

A fusion partner is typically for

A

solubility, monitoring expression, or crystallization

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9
Q

A cleavage site is for

A

tag/fusion removal

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10
Q

Co-expression of a protein with its binding partner can lead to a

A

stable complex more suitable for crystallization

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11
Q

Antibodies and nanobodies are often used to

A
  1. stabilize proteins
  2. serve as crystallization chaperones
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12
Q

Lysine methylation can improve crystallization by

A

changing surface charge properties of the target protein

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13
Q

Circular dichroism is used to measure contributions from

A

alpha-helices, beta-sheets and random coils

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14
Q

Light scattering can determine

A

molecular weight, radius of gyration, diffusion coefficient, and size distributions

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15
Q

ThermoFluor stability assay can determine

A

how stable an array of protein samples are

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16
Q

Small angle X-ray scattering can be used to calculate

A

a molecular envelope of a sample in solution

17
Q

NMR can help differentiate

A

a folded from an unfolded sample