Author: Anonymous

You can search for proteins that bind DNA using all of the following EXCEPT

Below is an SDS-PAGE (A) of an induced lysate (Lane 2) and a western blot (B) using an anti-target protein antibody. The protein was purified via affinity chromatography (Lanes 4-6). What is the molecular weight of the major contaminant (not the target protein) that was removed by the purification?

What conclusions could you draw from this peak from a size exclusion column?

Which technique would efficiently separate small organic molecules (like vitamins) for further use?

The gel below shows a protein before and after endo H treatment (100% efficiency). Based on this data, how many glycosylation sites does this protein contain?

You express a protein in E. coli at 37 °C, lyse the cells, and perform a western blot (below). Which of the following would be an appropriate next step?

The western blot of an SDS-PAGE below shows ARD1’s role in ubiquitination of proteins. The full-length ARD1 (1-574) is shown in the first lane, with other various constructs in the following lanes. Which of the following is TRUE?

Which of the following techniques can be used to identify where a protein binds in a DNA sequence?

What is the purpose of Tween-20 in the western blot washes?

What is the molecular weight of the band found in Lane 4 below?