The gel below shows an induced cell lysate of a his-tagged protein, with the pre-induced (lane 1), insoluble (lane 2), and soluble (lane 3) fractions. What technique should you use first to purify this protein?
Protein-protein and protein-drug interactions can be studied…
Protein-protein and protein-drug interactions can be studied on a massive scale using
Two proteins elute in fractions 30 and 40 of a size exclusio…
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. What would you expect if they interact?
A protein that can be acetylated has five domains (A through…
A protein that can be acetylated has five domains (A through E). Researchers deleted these domains in the western blot of an SDS-PAGE below. From this data, you can conclude that
What is the molecular weight of the band found in Lane 3 bel…
What is the molecular weight of the band found in Lane 3 below?
A technique that is useful in trying to identify new protein…
A technique that is useful in trying to identify new protein-protein interactions from a homogenate is
Which of the following is an advantage of in vitro protein e…
Which of the following is an advantage of in vitro protein expression?
Prior to running your sample in isoelectric focusing, you mu…
Prior to running your sample in isoelectric focusing, you must add
A calibration curve using protein standards is useful in
A calibration curve using protein standards is useful in
An experiment was performed to induce and purify the protein…
An experiment was performed to induce and purify the protein X. In the gel below, Lane 1 shows non-induced cells; Lane 2 shows induced cells; Lane 3 is purified MBP-X; Lane 4 is the protein after TEV cleavage; Lane 5 is the flowthrough after the cleaved sample has been run through an amylose column; Lane 6 is the purified TEV protease. Which band represents the protein of interest?