Tekmo

Let me Google that for you

That's a perfectly legitimate question that I myself asked while working in the lab.

First, check your sequence. It's really important that you know where your primer binds for several reasons: 1. You know if you will get undesired products (maybe it binds in more than one place or has a lot of similar binding sites) 2. You know what size band to expect 3. You know how long to run the extension part of the cycle (based on the amplified product length) I don't know why you only use a single primer unless it binds in two sites that are on opposite strands and face each other. PCR won't amplify exponentially unless you are copying both strands of the template. Also, I don't know how much DNA is typically produced from plant extraction, but if it normally produces a lot you could run that dna extract on a gel just to see if the extraction worked. But it is more likely that the PCR failed, since PCR (in theory) only needs a single strand of the template DNA present to work. Also, it's generally a good idea to always design your primers yourself. There are a lot of mistakes you can make with designing primers (I know I've made plenty of those mistakes) and designing them yourself will help you learn to catch potential problems early on. It's best to ask somebody you are working with for help with this but here's a good place to start if you wanted to do some learning on your own: http://www.premierbiosoft.com/tech_notes/PCR_Primer_Design.html

Let me Google that for you

The impression I got was that the brain could do everything it did with just classical physics. It's just a really complex computer.

The concentration of protons only equals the concentration of anions if the solution had no protons to begin with, or if the original concentration of protons in solution was negligibly small compared to the concentration of protons produced by ionization. It might not be the concentration of anions if you had a pH buffer in solution as well. Concentration of ionized is just referring to [A-]. That keeps the total concentration constant no matter how much disassociates.

I know Dr. George Georgiou from the University of Texas did a lot of work with directed evolution of proteins. Dr. Bill Degrado of University of Pennsylvania for his work in de novo design of proteins. I can't name much more than that off the top of my head.

The docking site of phosphinothricin on glutamine synthetase has already been crystallized. You can find the structure at the PDB under the code "1fpy". All you have to do is look at the structure to be able to answer your project's questions. PDB provides ways to view it in your browser, but if you have any questions on doing that, just ask.