Author: Anonymous

Which of the following would be best to study the glycosylation state of a protein?

You use bacterial two-hybrid to study proteins A and B below. If you randomly mutate protein A at the position noted,

Mass spectrometry can be used to determine all of the following EXCEPT

Hemoglobin contains 4 subunits (2 α, 2 β) of 141 and 146 amino acids, respectively. You would expect to see ______ band(s) on SDS-PAGE, and ______ band(s) on a native gel.

Two proteins elute in fractions 30 and 40 of a size exclusion column on their own. You mix them in equal molar ratios and run them over the same column, and you only see peaks in fractions 30 and 40. What would you conclude?

In chromatin immunoprecipitation, 

Does the gel below look as expected? Why or why not?

You perform SEC and run the fractions on an SDS-PAGE gel. The first SEC fractions would produce

When expressing proteins such as insulin, yeast may be more advantageous than E. coli because

Protein X is reported to decrease p53 levels. After treating cells with Protein X (+ lane) and adding anti-p53 and control antibodies, you see the following results. Which result indicates that Protein X decreases p53 levels?