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The exam will be cumulative. Approximately 20% of the exam will be on new material that we have covered since the last exam. This includes portions of Chapter 22 - 26. These questions will be more detailed than questions on the older material. There will be 5-10 questions asking you about biochemistry related disease handouts. The remaining 75% will be on material from previous exams (~25% from each exam). I may include diagrams and ask questions about them--consider the things that I emphasized. 

The exam will consist entirely of multiple choice problems (100 problems). If you are someone who routinely has trouble with this format, here are some helpful hints:

1. Read the question carefully. Think about what I am actually asking. Look for any key words such as NOT.

2. Go with your first instinct. Often second-guessing and over-analyzing your answer makes you change to an incorrect answer. Yes there will be answers similar to the correct one, otherwise it would be too easy, but these are not meant to confuse, but to be sure you know your stuff!

3. If you have never heard of a word before, it is the incorrect answer. In an effort to come up with four incorrect choices I often make up a word that sounds related to the topic at hand, but is a nonsense word. If it is unfamiliar from the text and lecture, don't chose that answer.

4. Use the process of elimination. Out if 4 to five possible choices, one is correct, one is a "toughie" --one I think you may confuse with the real answer, the other 2 to 3 are usually easily eliminated (see number 3). Try to get it down to 2, and then hey, you are down to 50% chance!

5. Please ask if you don't understand the question. I cannot give you the answer, but sometimes I can rephrase the question in a way that makes more sense to you. Also, I do make mistakes, I freely admit it, so don't hesitate to point them out.

This is the review sheet for the entire exam. Do try to keep in mind what are some of the bigger concepts that we have covered during the course. I know this is long, but I hope this is helpful. As usual, feel free to contact me with any questions you may have. Email: lrapp@stcc.edu Office phone: 755-5254

Exam 1 info

Proteins, Carbohydrates, Nucleic Acids, Lipids

Chapter 18: Carbohydrates

Exam 2 info

Chapter 19: Lipids

Chapter 20: Proteins

Exam 3 info

Chapter 21: Enzymes

	Allosteric regulation
	When is this involved? How does it work? Where does modulator bind?
	What is a zymogen?
	Example: pepsinogen,  prothrombin

	Irreversible
	Change tertiary or quaternary structure if enzyme/permanently inactivates
	Example: insecticides, nerve gas, penicillin, cyanide
	How do insecticides work? (what enzyme is inactivated?)

What are factors that influence enzyme activity? review graphs we discussed in class looking at the effect of pH, temp, substrate conc., enzyme conc., end product conc. on reaction rates. *I may draw a graph and ask a question.  what is meant by optimum ph? optimum temperature?

DNA Structure

	G, A, T, C = 4 nucleotides that make up DNA
	What are the three components of a nucleotide?
	Watson Crick model: Nucleotides are linked together (using dehydration synthesis reactions, of course!) to make a chain; two chains are held together by weak hydrogen  bonds to make a double stranded helical molecule.  Nucleotides joined by dehydration synthesis--bond holding nucleotides together along chain are phosphodiester bonds.
	A always pairs with T; G always pairs with C
	Be able to determine the second DNA strand if given a single strand of DNA
	RNA nucleotides = G, A, U, and C

DNA to Proteins  

	DNA ---->RNA----->Protein
	DNA, which contains genetic information, is stored in nucleus
	DNA is copied during TRANSCRIPTION into mRNA which can leave the nucleus

	A new RNA is copied from a specific DNA region according to base-pairing rules during transcription
	The information on mRNA is TRANSLATED into protein in the cytoplasm
	RNA nucleotides = G, A, U, and C.  What does U pair with during transcription?
	*Be able to make an mRNA sequence if given a DNA sequence, and the be able to "translate" this mRNA into protein using the genetic code. (Like the in-class exercise)
	AUG = start codon
	what is a codon?

	Be familiar with the GI tract and the following structures/organs involved in digestion (be able to recognize these structures in a diagram): -Mouth -Esophagus -Stomach -Intestine (duodenum, jejunum, ileum) -Liver -Pancreas -Gallbladder
	What is the difference between mechanical and chemical digestion?

What are dietary sources of carbohydrates?

Be familiar with the steps of carbohydrate digestion:

	Where does chemical digestion of carbs begin?
	What is salivary amylase and what does it do?
	How is the stomach involved in digestion of carbs?
	What is pancreatic amylase? Where is it from and where does it work?
	What happens in the jejunum (matase/sucrase/lactase)
	What is final "product" of carbohydrate digestion?
	Review figure 24.2
	What are the fates of the monosaccharides? -Immediate energy production (glucoseà glycolysis-à -à ATP) -Short (glycogen)/long term (lipid) energy storage -Synthesis of complex molecules (lipids/ribose/deoxyribose/glycoproteins)

	chemical digestion begins in stomach (gastric lipase)
	bile acts as emulsifier in small intestine; pancreatic lipase continues digestion of TAGs to MAGs and free fatty acids
	What is the role of micelles and chylomicrons in digestion of TAGs? (don't worry about structure--just know the they help transport out of intestinal cells and into bloodsteam)
	lipoprotein lipase hydrolyzes TAGs to glycerol and free fatty acids in bloodstream
	What are the final "products" of lipid digestion?
	Review figure 25.3

	Be familiar with the steps of protein digestion:
	Where does mechanical digestion of proteins begin?
	Where does chemical digestion of proteins begin?
	What chemicals/enzymes are involved in protein digestion in the stomach? (HCL/pepsinogen)
	What enzymes are involved in protein digestion in the duodenum? (enterokinase/trypsinogen/trypsin/chymotrypsin/carboxypeptidase)
	From where are they secreted? (pancreas, except for enterokinase, which is secreted from the duodenum)
	What enzymes are involved in protein digestion in the jejunum? (aminopolypeptidases). Where are they located?
	What is final "product" of protein digestion?
	Review figure 26.1
	Where are amino acids absorbed?

Be familiar with the terms metabolism, catabolism, anabolism

Be familiar with the overall purpose of , the citric acid cycle and the ETS *What is the central molecule that products of Carb/protein and lipid digestion are converted to and that feeds into the citric acid cycle?  See Chemistry at a glance figure p. 722 *what are the important products of the citric acid cycle in relation to energy production? See figure 23.16 SECTION D01 (MWF 11:15) ONLY:

You do not need to be familiar with the individual steps of these pathways Which enzymes in the citric acid cycle are under allosteric control?  What is the nature of this regulation? (inhibited or activated? by what?)

Where, specifically, in the cell does each process occur (citric acid cycle and ETS)?

Be familiar with the products of the citric acid cycle.

How many NADH, H+, FADH2  and GTP are generated in the citric acid cycle?

	For each molecule of NADH that enters the ETS, how many ATP are generated?
	For each molecule of FADH2 that enters the ETS, how many ATP are generated?
	How many H+ are transported across the membrane for each NADH and FADH2?
	How many H+ are transported across the membrane through ATP synthase for each ATP generated?
	What is meant by chemiosmotic potential? What does this do?
	By what process do glucose molecules enter the citric acid cycle?
	By what process do fatty acid molecules enter the citric acid cycle?