I have left up last semester's review sheet as some students find these useful. It will be updated for Spring 2010 2-5 days before the exam.
PLEASE BE ON TIME FOR THE FINAL EXAM--IT IS VERY DISRUPTIVE TO OTHERS TO COME IN LATE.
some small additions are in purple
Fall 2009 exam dates:
section DO1 (MWF 11:15): Friday Dec 18th 2:00-3:50
section DO2 (TTH 9:30): Tuesday Dec 22 8:00-9:50
If you would like to look at your previous exams, please stop by my office. I will be in my office the following hours:
Wednesday Dec 16 12:15-2:15
Thursday
Dec 17 9:15-2:15
Friday Dec 18th 9:15-3:50
( I will be in room and room 504 from 2:00-3:50, come see me there)
Monday Dec 21st
9:15-3:50 (
I will be in room and room 609 from 2:00-3:50, come see me there)
I will give you the exams to look over in a nearby room, and then you can return them to me. If I am not available during these posted hours, I will be leaving the exams in the lab technician's prep room (600) and you can ask to see them. Gail will allow you to look at them in a nearby room, and then you can return the exams to her. The exams will not be available outside of these posted hours. If you would like to request a different time, let me know and we can try to arrange an appointment.
Biochemistry BIOL-140 Final exam review sheet
The exam will be cumulative. Approximately 15% of the exam will be on new material that we have covered since the last exam. This includes portions of Chapter 12-15(23 - 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
Some General Info/review of Chemistry stuff:
 | What are the four most commonly occurring elements? |
| What type of bonds link atoms together to form molecules? |
| Why is carbon central on biological molecules? |
| What is a carbon skeleton? |
| How many bonds can Carbon form with other atoms? |
| How many bonds can Hydrogen form with other atoms? |
| How many bonds can Oxygen form with other atoms? |
| What are functional groups? |
| Be able to recognize certain functional groups |
| Hydroxyl (alcohol), carboxyl, amino |
| Know the four types of biological macromolecules. |
Proteins, Carbohydrates, Nucleic Acids, Lipids
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What are the elements that make up macromolecules? |
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Understand that the 3 of the macromolecules are built by bonding together smaller molecules, known as monomers |
| monomers link together to form polymers |
| Know which monomer makes up proteins, carbohydrates or nucleic acids. |
| Know which type of bond links amino acids, monosaccharides and nucleotides |
| Review dehydration synthesis. What does it do? Are water molecules used or produced? |
| Review hydrolysis. What does it do? Are water molecules used or produced? |
Chapter 7 (18): Carbohydrates
| What are dietary sources of carbohydrates? |
| Carbohydrates made up of simple sugar monomers called monosaccharides (glucose in particular). |
| What elements make up carbohydrates? How is this different than proteins and lipids? |
| Be familiar with the general functions of carbohydrates. |
| Are carbohydrates soluble or insoluble? |
| What are the three common monosaccharides? What is the relationship between them? |
| Be able to recognize glucose in either a ring or straight form |
| When is glucose in a ring form? |
| What is the difference between an aldehyde and a ketone? | |
| Be able to recognize a generic carbohydrate given its name (ex: aldopentose) like we did on the in-class worksheet | |
| Sugar’s names end in –ose | |
| What are the common disaccharides? What monosaccharides are they made from? | |
| How are monosaccharides linked together to form polysaccharides? | |
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| Know the structure and functions of the following polysaccharides and also
how they differ from one another. (are they found in animals or plants? are
they soluble in water? are they structural molecules or glucose storage
molecules? is it digestible by humans?) -Starch -Glycogen -Cellulose -Chitin |
| What enzymes break each of the disaccharides? |
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What is glycogenesis? Glycogenolysis? |
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what is the role of fiber in the diet? |
Exam 2 info
Chapter 8 (19): Lipids
| Lipids are macromolecules but are NOT polymers |
| Be familiar with the functions of lipids |
| Be familiar with the common properties of lipids |
| What are the dietary sources of lipids? |
| What elements make up lipids? How is this different than carbohydrates and proteins? |
| All lipids are hydrophobic (or amphipathic) what s meant by amphipathic? |
| Be able to recognize a fatty acid structure. |
| Know the difference between unsaturated and saturated fatty acids. |
| Be familiar with the difference between monounsaturated and polyunsaturated. |
| What are examples of lipids (in our diet) that contain each? |
| What is meant by the cis and trans isomers of fatty acids? Where do each occur? Which is more similar to a saturated fatty acid? |
| What is the difference between omega 3 and omega 6 fatty acids in terms of structure? |
| be able to write the abbreviation for a given fatty acid (for example, 18:1D6, 9) |
| Be familiar with the five categories of Lipids |
| What are Triacylglycerols? What are their functions? |
| What is the structure of a triacylglycerol? Be able to recognize. |
| How are triacylglycerols formed from their components? How many water molecules are involved? |
| What is the different between fats and oils? |
| What are the dietary sources of fats and oils?What are sources of both "bad' and "good" fats and oils? |
| What is meant by the term "essential"? essential fatty acids/ What are the two essential fatty acids? |
| What are the three types of Membrane Lipids? |
| What are phospholipids composed of? which part of the molecule is hydrophilic? hydrophobic? What |
| what is the general structure of cholesterol? What is its function in the cell membrane? |
| How do the three types of membrane lipids come together to form the plasma membrane? How are the lipids arranged? What other macromolecules are part of the membrane? |
| What is an emulsifier? What abut the structure of bile acids allow them to act as an emulsifier? Where are bile acids made and stored? |
| Messenger Lipids: Steroid hormones/eicosanoids |
| What are examples of steroid hormones? |
| What is the difference between how steroids and eicosanoids work? |
| What are examples of eicosanoids? |
Chapter 9 (20): Proteins
| What are some important functions for proteins in our cells? |
| Proteins are made up of monomers, called amino acids. |
| What are the parts of amino acids? |
| Be able to recognize the general structure of an amino acid. |
| How many different amino acids are there? |
| What elements make up proteins? How is this different than carbohydrates and lipids? |
| Be able to recognize (not draw) the following 3 amino acids: alanine, and glutamic acid, and lysine |
| What is a stereoisomer? What isomer is found in humans? |
| Ionization of an amino acid can occur at the amino group, the carboxyl group or both, depending on the pH |
| Review how alanine, glutamic acid, and lysine will ionize (which groups are charged?) at low pH, high pH, physiological pH |
| What is meant by essential amino acids? |
| How are amino acids linked together to form polypeptides? |
| What is a peptide bond? |
| Know the difference between the primary structure of a protein and the higher order structures (secondary, tertiary and quaternary) |
| Secondary -Due to H bonding between peptide bonds -Alpha helix, Beta pleated sheet (depends on R groups) |
| Tertiary -Due to bonding (hydrogen, electrostatic, disulfide, hydrophobic) between R groups |
| Quaternary -Due to bonding (hydrogen, electrostatic, disulfide, hydrophobic) between R groups -Involves more than one polypeptide chain |
| Be able to recognize which level of structure in a drawing |
| What is denaturation? What can cause denaturation? |
| What is the difference between fibrous and globular proteins? |
Exam 3 info
Chapter 10 (21): Enzymes
| Enzymes catalyze biological reactions |
| What types of macromolecule are enzymes? |
| how do enzymes accelerate reactions? |
| Be familiar with the terms substrate, enzyme-substrate complex, product, active site |
| Enzymes lower activation energy for reactions |
| Enzyme specificity (Absolute or relative) |
| Be familiar with the Lock and Key versus Induced Fit models of substrate/enzyme interaction |
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What is a cofactor? Metal ion, such as Mg+, Cu++, Zn++) Coenzyme (organic molecule, often vitamin derivatives such as NAD+ and FAD+ which are derived from vitamin B) |
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What is an apoenzyme? Holoenzyme? |
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Enzyme names end in –ase |
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Be familiar with the following general types
of enzymes and what they do: -Transferase -Hydrolase -Isomerase -ligase |
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Be familiar with alcohol dehydrogenase because
we used this example repeatedly Ethanol + NAD+ -ŕ acetaldehyde + NADH + H+ requires two cofactors: |
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metal ion: zinc |
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coenzyme: NAD+ |
| Allosteric regulation |
| When is this involved? How does it work? Where does modulator bind? |
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| What is a zymogen? |
| Example: pepsinogen, prothrombin |
Enzyme Inhibition
| Irreversible |
| Change tertiary or quaternary structure if enzyme/permanently inactivates |
| Example: insecticides, nerve gas, penicillin, cyanide |
| How do insecticides work? (what enzyme is inactivated?) |
Reversible Competitive
Structurally similar to natural substrate/compete with it for binding to active site
Examples:1.ethylene glycol is competitive inhibitor of alcohol dehydrogenase (see reaction above) and 2.sulfa drugs
Reversible
Non-competitive
Do not resemble substrate/bind away from active site
Examples: heavy metal ions (lead/mercury)
| What are factors that influence enzyme
activity?
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Chapter 11 (22): Nucleic Acids
DNA Structure
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| G, A, T, C = 4 nucleotides that make up DNA |
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| What are the three components of a nucleotide? |
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| 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. |
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| A always pairs with T; G always pairs with C |
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| Be able to determine the second DNA strand if given a single strand of DNA |
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| RNA nucleotides = G, A, U, and C
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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 |
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| A new RNA is copied from a specific DNA region according to base-pairing rules during transcription |
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| The information on mRNA is TRANSLATED into protein in the cytoplasm |
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| RNA nucleotides = G, A, U, and C. What does U pair with during transcription? |
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| *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) |
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| AUG = start codon |
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| what is a codon? What is tRNA? rRNA? What is a ribosome and what does it do?
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THE NEW STUFF:
| 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 is the cells main energy molecule? |
| What is the relationship between ADP and ATP? |
Chapter 13 (24): Carbohydrate Metabolism
| 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 13-2 (24.2) |
| What is the process that converts glucose to acetyl
CoA? |
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Chapter 14 (25): Lipid Metabolism
| 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 14-3 (25.3) |
| What is the
process that coverts fatty acids to acetyl CoA? |
Chapter 15 (26): Protein Metabolism
| 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 15-1 (26.1) |
Chapter 12 (23): Biochemical Energy Production
| Be familiar with the terms metabolism, catabolism, anabolism |
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Biochemistry Related Disorders:
I will ask some basic/general questions on the information sheets.Section D01: Lactose intolerance, Tooth Decay, Maple syrup Urine disease, Alkaptonuria, Jaundice, Lactic Acidosis
Section D02: Lactose intolerance, Tooth Decay, Maple syrup Urine disease, Marfan Syndrome, Alzheimers, cystic fibrosis