SDS polyacrylamide electrophoresis could be used to do which of the following?

a. determine the molecular weight of an oligomeric (multisubunit) protein

b. determine the molecular weights of subunits of an oligomeric protein

c. purify a monomeric enzyme in its active form

d. determine the folding state of a monomeric enzyme

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Reid WolffLv2

24 Dec 2018

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CHECK ALL ANSWERS THAT APPLY. THERE MAY BE MORE THAN ONE ANSWERFOR EACH QUESTION. Thank you!

You know the molecular weight of the monomeric Encprotein; however you would like to get an idea of what the pI ofthe protein is. From the following options, what is the best way toestimate that?

[ ] SDS-PAGE

[ ] Size-exclusion chromatography

[ ] 2-D gel electrophoresis

[ ] "Salt out"

Protein analysis: You are attempting to separate a60-subunit protein, Enc, from a mixture of other proteins. Eachmonomer has a molecular weight of 29 kDa. At pH 7.0, the proteinhas a net charge of -12. Which of the following options is the bestway to purify this protein?

[ ] âSalt outâ via ammonium sulfate precipitation and ionexchange chromatography

[ ] Ion exchange chromatography and size-exclusionchromatography

[ ] SDS-PAGE and affinity chromatography

[ ] âSalt outâ via ammonium sulfate precipitation and affinitychromatography

I have two purified samples of the enzyme PKA (ProteinKinase A). One sample is treated with cAMP (cyclic AMP), while theother other is not. The cAMP-treated sample shows 2 bands on anon-denaturing PAGE, whereas the untreated sample shows only 1band. What is the best explanation for this result?

[ ] PKA is activated by cAMP. The active enzyme would show morebands.

[ ] PAGE causes denaturation of the PKA.

[ ] cAMP unfolds PKA.

[ ] cAMP dissociates the regulatory and catalytic subunits ofPKA.

You have some protein sample and you want to quantify itusing a spectrophotometer. You take a small sample of protein andput it in a quartz cuvette, take a wavelength scan, and observeabsorbance intensity at 280 nm. Which of the following is likely tomake it so that you can analyze protein using aspectrophotometer?

[ ] Very concentrated protein sample

[ ] Proteins are composed of chiral molecules

[ ] The number of Trp and Tyr residues found in the amino acidsequence

[ ] All of the above

amberbadger529

A student given the task of purifying a protein found that the protein had a molecular mass of 400kDa when measured by gel filtration chromatography. (This technique involves the use of a column packed with material that functions like a molecular sieve. No harsh reagents are used so it preserves the native structure of the protein. ). The student wanted to confirm the purity of the protein by SDS-PAGE. When the protein was analyzed by polyacrylamide gel electrophoresis in the presence of SDS, 3 bands with the following molecular weights were obtained: 180, 160, 60kDa. However, the student realized that he/she forgot to add 2-mercaptoethanol to the sample gel buffer when it was made up. So the student ran the gel again, this time in the presence of SDS and 2-mercaptoethanol. This time, 3 bands were observed as before, however, the molecular weights were 160, 90, and 60kDa. If you were that student what would you conclude about this set of observations?

What would be the advantage of using two independent techniques (gel filtration and SDS-PAGE) to characterize a protein?

coffeeeagle50

1) You have separated two proteins, protein A that has migrated 3.5 cm and protein B migrated to a 4 cm distance from the loading point in the SDS-PAGE experiment. The tracking dye migrated to a distance of 6.5 cm. What will be the Rf value of protein B?

2) In paper electrophoresis, you separated amino acids based on charge. What is the variable this time? How do you know that there is only one variable in this separation?

3) You have an enzyme UTSase that is composed of three subunits. Two of the subunits are 34 kD and the other is 17 kD. How many bands will you see on an SDS-PAGE? Explain your answer.