Jump to content

Recommended Posts

Posted

After relentlessly bugging my profs about tips and methods to study for this test the only info i have gathered is that it has a ~65% failure rate and without purchasing one of the old test from ACS there is really no way to study for it. However, it was recommended to me that the semester I have to take this test to take Metabolism concurrently (which i am doing now) since around 40% of the test covers this subject. This test is worth 30% of my final grade and there will be no curve. Does ANYONE have any kind of advice, tips, hints, or anything of the sort that might be of some help? ANYTHING would be greatly appreciated:embarass:

  • 1 year later...
Posted

hey guys, just got out of the 2007 ACS biochem exam. I believe its the same one that is being used all through 2008.

 

 

 

I was told I took the 1 semester exam. My biochem course was 1 semester and this exam was supposedly the 1 semester exam. I believe this because there were no questions on the urea cycle or photosynthesis

 

 

 

for the 1 semester exam, it was not hard, it was not easy. It was medium. I had to self teach myself biochemistry, I mean the entire semester, and taught myself from a lehninger book and I feel I wasn't totally prepared. For a side note, for anyone familiar with ACS exams, this is def. easier than org chem ACS exam. Don't be in fear of something that gruesome... know your stuff you will be fine

 

 

 

Anyway, questions

 

 

 

Know glycolysis thoroughly, the enzymes involved. Which steps produce NADH.

 

What pathways and enzymes does ATP inhibit?

 

What is the use of the NADPH produced in HMP? Is it used in anabolic or catabolic reactions?

 

Recognize the STRUCTURES (not the functions) of biotin, TTP, THP, PPT? I wasn't sure what PPT was. You need to destinguish between them

 

Know the difference between competitive and non-competitive inhibitors and their effects on graphs

 

Know what is on the coordinates of the enzyme graphs that measure Km, Vmax

 

Know SDS-Page

 

Know PCR

 

If you are given a 4 small polypeptides amino acids (like glu-his-gly-arg), be able to recognize at a given pH the order those polypeptides will migrate to anode/cathode. Memorize your pkas!

 

BTW the one letter codes and three letter codes are given on the exam

 

Know how much ATP is produced from Kerb's and know where it is produced at (which steps)

 

Know in glycolysis and Kreb's cycle where NADH, FADH2, etc are produced

 

What is the difference between glycolysis and gluconeogenesis? (throroughly know difference in terms of structure, enzymes, etc)

 

Know translation in the sense, what will a point mutation do to amino acid sequence? What will a deletion do? Etc.

 

Whats the differences between bacterial and eukaryotic DNA replication?

 

Know translation, what are promoters, etc?

 

What are the enzymes in the pyruvate dehydrogenase complex?

 

What are the end products of the Kerb's cycle ONLY?

 

In globular proteins, what might be used to break cys redisues? If you know, know a lot about that answer!

 

In hemoglobin, know generally how O binds, what does 2,3BPG what about the differences in going from the T to the R state?

 

Know the basic difference between an anabolic and catabolic pathway (which is reductive, oxidative?)

 

Whats a thioester bond?

 

Which lipids have glycosidic linkages?

 

What are the allosteric effectors of the steps in the Kreb's cycle?

 

 

 

OK guys thats about what I remember for now. If anyone has more questions just post them i will check in every once and a while

 

 

 

I am just trying to give a study guide here because there isn't one. There is more than just this stuff, and every thing I mentioned know it thoroughly! The questions are asked in a way that you should understand it just not have things memorized!

 

 

 

Hope this helps!

Posted (edited)

In regards to the structure and binding of haemoglobin, and its allosteric properties, should one know the graphic method of ataining the Hill coefficient? Should one also know how to analyse a double reciprocal plot of enzyme catalysis? And is there anything on the test in regards to the structure and function of extracellular proteins?

 

ps: Don't worry, I'm not taking the test myself...yet. I'm just interested in terms of what one is allowed to skim over, in contrast to that which is necessary. (Despite their necessity, pKa values by nature, I find to be a nuisance.)

Edited by Theophrastus
Consecutive posts merged.

Create an account or sign in to comment

You need to be a member in order to leave a comment

Create an account

Sign up for a new account in our community. It's easy!

Register a new account

Sign in

Already have an account? Sign in here.

Sign In Now
×
×
  • Create New...

Important Information

We have placed cookies on your device to help make this website better. You can adjust your cookie settings, otherwise we'll assume you're okay to continue.