When designing an affinity chromatography process for a new protein, what is a critical first step?

Why does activity alone not indicate the purity of a protein sample?

Why is achieving maximal and constant specific activity significant in protein purification?

Which purification technique is most likely to result in the highest increase in specific activity?

In a chromatogram, what does a higher peak indicate about the concentration of a molecule?

In reverse phase HPLC, which type of molecules elute first and why?

What does a longer elution time on a chromatogram indicate about a molecule's interaction with the stationary phase?

In Beer's Law, what does the ratio of incident light (I₀) to transmitted light (I) represent?

Which of the following factors would increase the absorbance of a solution in a spectrophotometer?

A mixture of proteins and nucleic acids is analyzed. How can the absorbance spectrum be used to determine the relative concentrations of these biomolecules?

A protein with a net negative charge is placed in a native PAGE gel. In which direction will it migrate?

Why is retaining native protein properties important in native gel electrophoresis?

How do proteins with identical masses but different charges behave in a native PAGE gel?

Why is the relationship between the log of molecular weight and relative migration in SDS-PAGE considered linear?