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TLS Online TPP Program

#Question id: 27984

Correct order of Electron transfer through Complex IV is

#Unit 1. Molecules and their Interaction Relevant to Biology

  1. cytochrome c  → Fe-Cu center → CuA  →  Oxygen now binds to heme a3 converts  →   O2 to two molecules of water

  2. cytochrome c  → heme a3  →  CuA →  Oxygen now binds to Fe-cu center converts → O2  to two molecules of water

  3. cytochrome c → CuA → Fe-Cu center → Oxygen now binds to heme a3 converts  → O2 to two molecules of water

  4. Fe-Cu center → CuA → cytochrome c → Oxygen now binds to heme a3 converts → O2 to two molecules of water

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TLS Online TPP Program

#Question id: 18846

#Unit 13. Methods in Biology

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.
TLS Online TPP Program

#Question id: 18847

#Unit 13. Methods in Biology

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?
TLS Online TPP Program

#Question id: 18848

#Unit 13. Methods in Biology

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

#Question id: 18849

#Unit 13. Methods in Biology

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

#Question id: 18850

#Unit 13. Methods in Biology

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

#Question id: 18851

#Unit 13. Methods in Biology

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?