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Chemistry
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13 Dec 2019

1. Why are the proteins from the polyacrylamide gel transferredto a nitrocellulose membrane for this experiment?

2. Explain the purpose of each of the following in the westernblot:

Blocking solution

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Hubert Koch
Hubert KochLv2
17 Dec 2019

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Related questions

A protein of interest needs to be separated from a mixture of proteins for amino acid sequencing. It is known that the protein of interest is highly enriched in lysine residues compared to the other proteins in the mixture. Which of the following techniques will be most effective in isolating this protein?

options:

a)

gel-filtration chromatography
b)

SDS-polyacrylamide gel electrophoresis
c)

mass spectrometry
d)

cation exchange chromatography
e)

anion exchange chromatography

2. Consider a mixture of three peptides. The three peptides have the following primary structure:

A) asp-asp-val

B) glu-asp-glu

C) val-val-lys

Determine the net charge of each peptide at pH 7. From this, in what order will these peptides elute from an anion exchange column at pH 7?

options:

a)

A will elute first, followed by B then C.
b)

B will elute first, followed by C then A.
c)

C will elute first, followed by A then B.
d)

B will elute first, followed by A then C.
e)

Not enough information is provided to determine the elution order.

Which of the following is not associated with the folding of a protein into its native conformation?

options:

a)

Molecular chaperones prevent folding intermediates from aggregating.
b)

Folding of proteins is a relatively slow process as the stabilization of the molecular structure depends solely on salt bridge interactions which take time to form.
c)

The major driving force for protein folding is the overall increase in solvent entropy. This increase in solvent entropy is a result of the strong interactions between water molecules that lead to the association of nonpolar side chains and subsequent collapse of the molecule into a more compact shape.
d)

Hydrogen bonds contribute to the cooperativity of folding and help stabilize the native conformations of proteins.
e)

All of the above are associated with the folding of a protein into its native conformation.

2 . A protein of interest needs to be separated from a mixture of proteins for amino acid sequencing. It is known that the protein of interest is highly enriched in lysine residues compared to the other proteins in the mixture. Which of the following techniques will be most effective in isolating this protein?

options:

a)

gel-filtration chromatography
b)

SDS-polyacrylamide gel electrophoresis
c)

mass spectrometry
d)

cation exchange chromatography
e)

anion exchange chromatography

Question #2 and please explain how to calculate the differences with buffer pH levels

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