Which of the following are the two main components of column chromatography?

How do different affinities of components for the mobile and stationary phases result in separation during column chromatography?

Why might column chromatography be considered less cost-effective compared to other protein purification techniques?

What is the primary purpose of ion-exchange chromatography in protein purification?

In a cation exchange chromatography column, which proteins elute first and why?

How does ion-exchange chromatography differ from other types of chromatography?

Which of the following is an example of a positively charged stationary resin used in anion-exchange chromatography?

What is the relationship between ionic interactions and protein movement in an anion-exchange chromatography column?

What is a potential disadvantage of using anion-exchange chromatography for protein purification?

Given a mixture of proteins, how would you expect the elution order to change if the pore size of the beads is increased?

What is a potential limitation of size exclusion chromatography in protein purification?

A student claims that in both size exclusion chromatography and gel electrophoresis, smaller molecules elute first. How would you correct this misconception?

In an affinity chromatography setup, what is the role of the stationary phase?

What is a key advantage of using soluble ligands to elute proteins in affinity chromatography?