PracticeExam2005 - These questions are from an old Biochem...

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These questions are from an old Biochem exam from this University. They are only meant to exemplify the types of questions that you can expect, to the level of detail you may expect. There may be different numbers of each kind of question and different material on your exam. There may be a different number of total questions. The format will be the same. DO NOT ANSWER THESE UNTIL YOU HAVE SPENT TIME STUDYING. Identify the amino acids in this portion of a peptide at the right 1. 2. 3. a. P a Glutamine a Glu b. R b Serine b Gln c. G c Alanine c Ala d. Y d Lysine d Asp e. W e Arg e Arg 4. I have a tube of water with a tube containing a little of the peptide above. How could I identify which tube had the peptide? a. Treat the samples with peptidase and run SDS-PAGE b. Put the tubes in a spectrophotometer and dial it to 260 nm c. Look for absorbance of ultraviolet light at 280 nm d. Treat the samples with Dithiothreitol or Performic Acid and run an SDS-PAGE e. Place a spot of each sample on a silica plate and run thin layer chromatography 6. The two molecules at the right are a. Diastereomers b. Configurational isomers c. Epimers d. Enantiomers e. Conformational isomers 7 Which carbon of this disaccharide would most likely participate the branched configuration of amylopectin? a. 1 b. 2 c. 3 d. 4 e. 5 1 1 2 3 2 Rest of
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8. Based on this graph, this enzyme would likely… a. Bind an inhibitor that changes Vmax and not Km b. Bind an inhibitor then a substrate, or a substrate then an inhibitor c. Generate a sigmoidal velocity plot d. Change only the amount of product formed and not how fast it was formed e. Display second-order rate kinetics 9. This data indicates a. A Competitive Inhibitor b. A Non-Competitive Inhibitor c. A Mixed Inhibitor d. An Uncompetitive Inhibitor e. A Mechanism-based Inhibitor 10. The Y-intercepts of the lines on this graph indicate a. - Km b. - 1/Km c. - Km/Vmax d. The substrate concentration at which the enzyme is transforming Substrate into Product at half the maximal rate e. 1/Vmax 11. Which type of bond stabilizes the quaternary structures of chitin and cellulose, making them rigid? a. Hydrogen bonds b. Hydrophobic interactions c. Peptide bonds d. Van der Waal’s interactions e. Glycosidic linkages 12. Which of the following is a significant physical characteristic of Cholesterol? a. Completely hydrophobic, explaining how it associates with membrane acyl chains b. Completely hydrophilic, explaining how it improves membrane fluidity by associating with the lipid polar head groups c. It is Amphoteric d. It is Amphipathic e. None of the above is a characteristic of cholesterol 13. Which of these definitions best describes a prosthetic group ? a. That part of an enzyme which binds H+ during acid-base catalysis
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This note was uploaded on 01/06/2010 for the course MCDB 310 taught by Professor Walter during the Fall '09 term at University of Michigan.

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PracticeExam2005 - These questions are from an old Biochem...

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