exam2b - BIOL/CHEM 3361 Spring 2011 Name_ EXAM 2 FORM B...

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BIOL/CHEM 3361 Name__________________________ Spring 2011 EXAM 2 FORM B Place your name at the top of this page of the exam. On the F-1712 Scantron form, use a no. 2 pencil to enter your test form designation, i.e., A or B. Also print and encode your name and your UTD ID (starting in the first column on the left and leaving the last spaces blank). Leave phone number, code and subject score sections blank. Select the best answer for the following multiple-choice questions and enter the corresponding letter on the Scantron sheet. You may use these test pages to make notes and work problems. You may use a non-graphing calculator or a graphing calculator you have cleared of all stored data. When finished, turn in this exam along with your Scantron sheet. 1. A measure of the specificity and efficiency of an enzyme is given by a. k cat /K m b. k cat [E] total c. k 1 /k -1 d. (k -1 + k cat )/k 1 e. the rate of catalysis at low [S] 2. Lineweaver-Burk plots (aka. double reciprocal plots) can be used to a. determine K m values b. distinguish between single and double displacement reaction mechanisms c. distinguish between competitive and noncompetitive inhibitors d. determine K I if [I] is known e. all of the above 3. Post-translationally modified amino acid residues in a protein are part of the protein’s a. quaternary structure b. tertiary structure c. supersecondary structure d. secondary structure e. primary structure 4. Which of the following enzymes is categorized as a hydrolase? a. trypsin b. glucokinase c. V8 protease d. a & c e. all of the above 5. Which of the following statements is true about competitive inhibition? a. V max is unchanged b. K m is unchanged c. V max and K m increase d. V max and K m decrease e. K I is the same for E and ES
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6. If a carboxylase (Mr 40,000) at a concentration of 0.1 μ g/ml and one active site per molecule has a V max of 0.3 x 10 -5 M/min, what will its turnover number be? a. 1.2 x 10 2 /min b. 1.2 x 10 3 /min c. 2.1 x 10 3 /min d. 4.8 x 10 3 /min e. 5.1 x 10 4 /min 7. An enzyme has an apparent K m of 2 x 10 -3 M and a V max of 1 x 10 -4 moles/min. in the presence of 1 x 10 -3 M competitive inhibitor (K I = 1 x 10 -7 M). What is the true K m of the enzyme? a. 2 x 10 -7 M b. 2 x 10 -6 M c. 2 x 10 -5 M d. 2 x 10 -4 M e. 2 x 10 -3 M 8. The active sites of pepsin and the HIV protease contain a. two aspartate residues that have identical pKa values b. two aspartate residues that form a LBHB c. a serine that forms an unstable acylated intermediate d. an EHS catalytic triad e. a lysine that forms a Schiff base during catalysis 9. A β hairpin or meander is a type of a. sheet structure b. domain structure c. secondary structure d. super-secondary structure e. random coil 10. How many amino acids are there per repeat of an α -helix? a. 2
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This note was uploaded on 02/08/2012 for the course CHEM 3361 taught by Professor Marsh during the Spring '11 term at University of Texas at Dallas, Richardson.

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exam2b - BIOL/CHEM 3361 Spring 2011 Name_ EXAM 2 FORM B...

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