practice_final_2007

practice_final_2007 - Name: Last First Short Answers 1. (6...

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Name: Last First 1 Short Answers 1. (6 pts) For each of the following, write the one letter code of the single common amino acid that best fits the description. Has no side chain. Has a total of two nitrogen atoms and four carbon atoms. The side chain readily react with iodoacetate and iodoacetamide. The smallest amino acid that has an alcohol group. The amino acid with the side chain attached to the α -amino group Side chain does not ionize, and includes an atom other than C, H, O, or N. 2. (5 pts) Name and briefly define four types of noncovalent interactions that occur between biological molecules. 3. You are familiar with the Michaelis Menten plot of Vi vs. [S]. Draw this plot and show how one can find Vmax and Km from it. Also, give the definition of Ks, and compare it to K M.
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Name: Last First 2 4. (9 pts) Answer the following questions for the peptide shown below. a) Write the name of this peptide using one letter amino acid abbreviations. b) What would the charge on this peptide be at pH 14? c) What would the charge be at pH 0? 5. (12 pts) Answer the following questions for the phospholipid drawn below. O O O P HO O O NH 2 O O a) What is the name of the 3-carbon molecule that forms the backbone of the lipid? b) What are the names of the fatty acids in this lipid? c) What is the general name of this phopholipid (not considering the names of the fatty acids)? e) What is the net charge of this lipid at neutral pH ? 6. (6 pts) What volumes of 0.1 M acetic acid (pK a = 4.8) and 0.1 M sodium acetate must H 2 NC HC CH 3 H N O CH C CH 2 H N O SH CH C CH 2 H N O OH CH C CH 2 H N O CH 2 CH 2 NH C NH 2 NH CH C CH 2 OH O N NH
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Name: Last First 3 be used to make 1 L of 0.1 M acetate buffer pH 5.1? Show all calculations. 7. Derive the Henderson-Hasselbalch equation from the expression for K a , and sketch the plot it describes (pH against amount of NaOH added to a weak acid). On your curve label the p K a for the weak acid, and indicate the region in which the buffering capacity of the system is greatest.
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Name: Last First 4 8. (8 pts) An enzyme catalyzes a reaction at an initial velocity of 20 μM/min when the concentration of the substrate is 0.05 M. The K M for this substrate is 10 -4 M. What will the initial velocity with the following concentrations of substrates? Show all calculations.
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This note was uploaded on 05/04/2008 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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practice_final_2007 - Name: Last First Short Answers 1. (6...

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