So we loaded some samples of tagged spectrin onto a gel last night in lab, along with unbound plasmid bits, wild-type bacteria, intact fusion protein, and the fusion protein piece cleaved off the tagged spectrin. Tag was "GSF." In a lab manual discussion that included GST, GSH, and an entire alphabet soup of other stuff, it took me until yesterday morning to realize the GFP = Green Fluorescent Protein. Er, yeah. Not yet another gluta-something, then.
I think I did well on the quiz; I spent a ridiculous amount of time hitting myself repeatedly over the head with a hammer - oops, I mean re-reading all the material I had - to make sure I understood *what* we were doing and *why* we were doing it, plus as much of how it all works as I could manage. So, hey, SDS partially denatures proteins and gets them to lie flat so you can evaluate comparative sizes when you run them through a gel! Gel not agarose for this experiment; gel was a polyacrylamide. The course info simply said, it's a polyacrylamide and it has better resolution because it can be made with smaller pores. The trouble was that the quiz asked, what're the other ingredients in the gel (choose from following list)? and what happens with a higher T ratio?
No idea. So I guessed, um, well the choice that contained "acrylamide" makes sense, 'cause it's poly-acrylamide, but...what the hell is T? And I spent some time today searching through all the course material, and then on Google and such trying to figure it out. I found lots and lots of polyacrylamide gel recipes! Boy, if I ever want to make up a gel, I am so ready! Gel this, gel that, gel all over the place!
So now I wonder, hm...what would happen if I ran an electrophoresis with actual Jello...
Silly weasel. But still, citric acid, glucose, a semisolid matrix structure - it has potential, doesn't it? perhaps as the most ridiculous undergrad research project ever? to go nicely with my Most Boring Paper Ever?