Which one is the incorrect conclusion of Anfinsen’s eperiments?

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#Question id: 18846

#Part-A Aptitude & General Biotechnology

For an application where you require a sample of your target protein at high purity, what would be a good purification strategy? Assume that your starting point is E. coli cells in which the target protein fused to an affinity tag has been over-expressed.

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#Question id: 18847

#Part-A Aptitude & General Biotechnology

You know that the protein you want to purify from a natural source forms a multimer with multiple sub-units giving a molecular weight in solution much bigger than visualised denatured on SDS-PAGE. There is only a small amount of the target protein in the total protein sample. Which of the following is an appropriate purification strategy?

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#Question id: 18848

#Part-A Aptitude & General Biotechnology

You find that your protein sample loses activity during storage. What can you do about this?

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#Question id: 18849

#Part-A Aptitude & General Biotechnology

Which of these techniques is often considered a suitable "polishing" step in a protein purification strategy?

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#Question id: 18850

#Part-A Aptitude & General Biotechnology

Which of these chromatography types are suitable as a "capture" step in the purification of non-tagged proteins?

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#Question id: 18851

#Part-A Aptitude & General Biotechnology

Nickel-NTA (Ni-NTA) chromatography is a popular affinity chromatography method for the purification of histidine-tagged proteins. However, SDS-PAGE of the eluted protein can show bands in addition to your target protein. How might you improve this purification step?