I was looking through the forums to see if there is any advice on how to study for biochem I. There doesn't seem to be much advice, mostly people talking about when or if they are taking the right biochem class. I am really struggling, 1st exam I got a 40%. I really need to do well. I don't understand how to study for this class. There is so much material. Am I trying to study too much by trying to study all of it? I think for most part I tried to do straight memorization off the slides, but that did not work.
I don't understand what people mean when they say learn important concepts or big ideas? How do I tell what to learn and what to avoid off the slides?
-some of the threads here were talking about drawing out the cycles but there is gotta be more than that.
-do practice problems and practice exam( but if I am not studying correctly it doesn't make sense)
I have a book I read the chapter for the exam.
I really frustrated I don't understand how to study for this class, there is so much material.
Thanks for the help
What is being taught for the semester? What is listed in the syllabus from beginning to end? How is the class is structured in general? Horrible teacher?
I don't know what was on your first test, but I am guessing that it was over the basics of amino acid and protein structure, some acid base chemistry, maybe replication, general review, etc.
Also.....
1. What type of questions did you get wrong in the first test? What prevented you from answering it?
2. What type of questions did the rest of the class get wrong? Why?
3. Is the teacher very horrible?
I am
guessing that you are going over protein purification and Kinetics at this moment and your teacher was really horrible at teaching it like mine.
Is he giving you a lot of info and you don't know what to memorize?
Compare what your teacher told you about protein purification/Kinetics and compare it with my list below. Does it make more sense this way?
Protein purification:
1. Pretend you are in Lab, and write down what needs to happen in order to purify a protein sample.
example:
-Release the protein from your sample
-Separate the mixture from solids and liquid
-Chromatography,etc.
-kinetic tests
-purification table
2. Next to it on another column, how accomplish this.
example:
-To release the protein from your sample (say liver), you need to put it in a blender with tris-buffer, on ice, with EDTA, beta mercaptoethanol,etc.
-To separate your mixture, pour it through cheese cloth to remove insoluble stuff, centrifuge,etc
-size exclusion chromatography, affinity chromatography, nickel column, etc.
-test for activity and use enzyme kinetics
3. Third column, white down WHY, you did the steps and HOW it works.
example:
During release phase
-Proteins are fragile, so you use buffer and ice to keep it stable. Tris is used because it was near pKa (you looked it up before exp) and cheap. This step also release enzymes that will lyse your protein so you use EDTA to bind to metals, since these enzymes usually requires some co-factor to function.
Separation phase
-cheese cloth and centrifuge to separate the crap that got released
Chromatography
-separate by size, shape...state how it does this, and how it works
-affinity...explain why you did this and how it works
The idea is that if you can actually perform protein purification in real life, and the reason how/why the steps are done, then you basically know it. It doen't matter how much random info he seems to throws at you, because you can always refer back to how you did the experiment and why.
Again, I am just trying trying to figure out what your class is teaching and I only took a guess at what you are learning right now and why you are having problems.
Gonna need you to tell us what you are learning and what kind of problems you have.
