You’re working with an MBP-p53 fusion protein, which is linked by covalent peptide bonds. You would expect to see ______ band(s) on SDS-PAGE, and ______ band(s) on a native gel.

A protein has a pI of 5, and is in a buffer at pH 7. What type of column should it bind to?

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

In the phage vector induction system,

You attempt to express a large protein using yeast cells, but the protein did not properly fold with this system. Which of the following is the appropriate next step for achieving successful protein expression?

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

Why is a solubility test important before ion exchange chromatography?

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?

What is the purpose of adding EDTA to a lysate?