CHE 2100 Fall 2012
General Organic & Biological Chemistry Review V
1. What is the minimum number of carbon atoms in an a-amino acid?
2. From the list of amino acids below, identify the following structures:
Alanine, Cysteine, Serine, Phenylalanine
3. In your own words, explain what a Zwitterion is.
4. Circle the amino acid below that you would expect to have the largest pI, isoelectric point.
5. How many amino acids have acidic side chains?
6. Draw the hydrolysis reaction of a pair of amino acids.
7. How many atoms form the “backbone” of the repeating unit of a polypeptide?
8. If the following pentapeptide is put in a gel electrophoresis unit with buffer at pH 3, will it migrate towards the positive or negative electrode?
9. What are the two most common forms of protein secondary structure?
10. When naming a polypeptide chain, you begin at the ______and go towards the ______.
11. The identity of the R groups contributes most significantly to the ______structure of proteins.
12. Explain why soap would effectively denature many proteins.
13. Draw the following molecules:
2-amino propanoic acid 2-Amino-3-(4-hydroxyphenyl)propanoic acid
Do they look familiar?
14. What are three roles of proteins in the body?
15. Explain what is wrong with the following statement: “Enzymes shift the chemical equilibrium to more heavily favor products.”
16. If an enzyme requires a non-protein additional element to function, that additional element is called a ______.
17. Why does having an enzyme recognize the transition state result in lowered activation energy?
18. Given the graph of enzyme kinetics below, estimate the Km.
19. In the reaction mechanism of acetylcholinesterase, which product is temporarily covalently bound to the enzyme?
20. In competitive inhibition, does the inhibitor bind to the active site or to an allosteric site? Is this an example of reversible or irreversible inhibition?
21. Name 2 examples of commercially used enzymes and what products they help create.
22. Draw a Lineweaver-Burke plot for a typical enzymatic reaction. Label where you would find the KM and Vmax.
-- We may reach the following material, depending on lecture progress. If we do not, it will help you prepare for the final exam.---
1. Describe how DNA is compacted so that the ~ six feet of DNA can fit into a single cell’s nucleus. What are the key levels of structure, and what proteins assist in this process?
2. Draw the structure of a single nucleotide of DNA, with 5’ phosphate and free 3’ hydroxyl. You may use the word “Base” instead of drawing a heterocyclic base.
Circle the functional group that would be different if this was RNA.
3. For the four nucleotides (adenine, cytosine, guanine, and thymine), describe each as either a purine or pyrimidine.
4. If a given sample of DNA contains 30% Cytosine, what percentage of the DNA is Adenine?
5. The two strands of the double helix of DNA are held together by what sort of bonds, between what part of the nucleotides?
6. What are the central molecules, and processes, of the Central Dogma of Molecular Biology?
7. What is the product of the process of transcription?
8. What molecule serves as a key “adaptor” between nucleic acids and amino acids?
9. What are introns and exons? Which is removed in the process of splicing, and why?
10. Approximately how much of the human genome codes for proteins?
11. What is a primer? How many primers are needed to perform the polymerase chain reaction?
12. If you begin PCR with 1 molecule of template DNA, after 5 cycles, how many total copies of DNA will you have?
13. What are “silent mutations”?
14. What are three causes of DNA mutation?
15. Given this pattern of results for a DNA fingerprinting experiment, which man is likely the father of the child?
16. What key piece of evidence was used to help elucidate the structure of DNA? Describe the 3-D structure of DNA.