Final Exam Answers

Final Exam Answers - Net ID KEY BIOBM 3310 FINAL EXAM 1 2 3...

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Net ID KEY BIOBM 3310 FINAL EXAM 12/11/09 1. _________ 2. _________ 3._________ 4. _________ 5. _________ 6. _________ 7. _________ 8. _________ 9. _________ 10. ________ 11. ________ 12. ________ 13. ________ 14. ________ 15. ________ 16. ________ 17. ________ 18. ________ 19. ________ 20. ________ 21. ________ 22. ________ 23. ________ 24. ________ 25. ________ ____________ TOTAL (140 possible pts) WRITE/PRINT LEGIBLY . IF WE CAN'T READ IT, WE CAN'T GRADE IT! PRINT NAME (LAST, FIRST) ON THE BACK TOP OF THE LAST PAGE ONLY
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A. Questions about drawing molecules 1. (6 pts) Draw the structure of the disulfide-linked dimer, (Gly-Cys) _ (Gly-Cys). R groups: Gly, H; Cys, CH 2 SH; at pH = 7. Show all of the bonded atoms. (The dipeptides are only linked by a disulfide). 2. (3 pts) Start with N 2 and draw three additional molecules showing increasing levels of reduction . Draw all bonded atoms. Do not bother to name the molecules. N N NH=NH NH 2 -NH 2 2NH 3 B. Questions about structure and charge 3. (8 pts ) The structure of γ -aminobutyric acid, a neurotransmitter, is shown below together with pKa values of its ionizable groups. H 3 N + CH 2 CH 2 CH 2 COOH a. What is the approximate overall charge on this molecule at the following values of pH: pH = 2 ___ +1 ___ pH = 7 ___ 0 ___ pH = 12 ___ -1 ___ b. When γ -aminobutyric acid has a net charge of zero, would it pass through a lipid bilayer at a rate that is FASTER SLOWER ABOUT THE SAME compared with a molecule of butyric acid at pH = 3? Circle your answer. 4. (3 pts) Briefly ( very very briefly ) list 3 ways in which tropocollagen structure is different from the structure of an α -helical protein: NO α -HELIX! DIFFERENT PHI,PSI VALUES TROPOCOLLAGEN IS A TRIPLE HELIX UNLIKE THE α -HELIX, LOTS OF PROLINE IN TROPOCOLLAGEN 10.0 4.0
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MANY MODIFIED PROLINES AND LYSINES 5. (8 pts) In the blank Ramachandran Maps on the right, SHADE IN the answers to the questions below. e.g. The dotted ellipses indicate the only regions having zero steric hindrance. a. The observed φ , ψ values for a typical protein that has helices, sheets, turns, and loops. b. The observed φ , ψ values for Mb. c. The observed φ , ψ values for a protein that is denatured and completely unfolded in 8M urea. d. The observed φ , ψ values for poly(Ala), the second- smallest of the amino acids.
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2 4 6 8 10 12 14 CH = CH -CH 2 -CH 2 - NADPH NADP + 6. (4 pts) Draw the graph of V vs pH for an enzyme that has both a Lys (pKa 10) that must be protonated, and a Glu (pKa 4) that must be unprotonated for rxn to be catalyzed. Label axes; show numerical values on the x-axis. | | | | | | | | | C. Questions about control of metabolism 7. (4 pts) Answer the following questions about mitochondrial ATP Synthase: a. How many active sites for ATP synthesis are present in each entire enzyme? _ 3 _ b. Give the Greek letter name or symbol for the subunit that rotates within
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This note was uploaded on 01/01/2012 for the course BIOMG 3310 taught by Professor Feigenson during the Fall '11 term at Cornell.

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Final Exam Answers - Net ID KEY BIOBM 3310 FINAL EXAM 1 2 3...

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