Guanidine-HCl and urea

The proteasome degrades ubiquitinated proteins. You treat cells with a proteasome inhibitor (+ lane), and visualize with an anti-ubiquitin antibody. What would be the expected results of inhibitor treatment?

Why aren’t native gels typically used to determine the molecular weight of proteins?

A chaperone and histone interact. Researchers mutated the chaperone as shown in the western blot of an SDS-PAGE below. Which amino acids are essential to the chaperone/histone interaction?

Which of the following is FALSE about protein induction?

A technique that allows you to determine the thermodynamics of protein-protein interactions is

To identify a protein on a 2D gel, you can perform all of the following EXCEPT

You express a protein using both the Ptac and phage systems in E. coli and run the pre-expressed and induced samples on a gel (below). What can you conclude?

You are studying a tetramer that consists of a 20 kDa homodimer and a 30 kDa homodimer. You would expect to see ______ band(s) on a native gel and ______ band(s) on an SDS-PAGE.

What is the disadvantage to fusing a target protein to GST?