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Chemistry
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12 Dec 2019

You have a mixture of peptides with the following amino acid sequences:

TYWSF

TEDSE

KAGFELCRNEDACEF

It will take at least two different chromatography columns to separate the three proteins from each other. Which non-denaturing purification methods do you use? Please explain, specifically, comment on which techniques will effectively separate which peptides from each other. Thanks.

A. Hydrophobic interaction column and a size exclusion column
B. Cation exchange column and a metal affinity column
C. Size exclusion column and a chitin affinity column
D. SDS-PAGE and an anion exchange column

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Beverley Smith
Beverley SmithLv2
13 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.

Dr. Kornberg, a Nobel laureate, recruited you to work in hisresearch lab. He assigned you a project to completely isolate andcharacterize a newly discovered native protein, smoothase. Hebelieves that his protein causes wrinkles to disappear. Preliminarystudies were performed and the results are listed below.
a) The protein bound to a phenyl sepharose column at pH 8.0.
b) Reducing SDS-page analysis resulted in proteins at about 40 and55 kDa.
c) Gel filtration chromatography resulted in a protein at about 135kDa.
d) The protein interacts with a nickel affinity column at pH7.
e) The protein interacts with an anion-exchange column at any pHvalue above 6.0 while it interacts with cation-exchange column atany pH value below 5.0.

A) Describe ALL the characteristics of smoothase that you candetermine from the preliminary data listed above. Be sure toexplain your reasoning.
B) Design a step-by-step purification scheme for smoothase usingthe techniques listed in a-e above and be sure to include any stepsneeded to prepare the samples for the next step and othercomponents (i.e. molecules) needed for efficient elution.

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