Fall 2005 Practice Exam Answers

Fall 2005 Practice Exam Answers - ,tbt "--' '...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full DocumentRight Arrow Icon
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: ,tbt "--' ' , 1,9,r, tt sohr l l l | ,o' I I Biology 31 1 2005 Midterm l('),r, NAME- Questions' nswer all on scantron A I Rest of peotide ldentify the amino acids in this portion of a peptide at the riqht 1 . Wr I r lu-ct'cH;{ }0H ) l l o = C W i i I ,,i",. .t c . " @ e. P R G Y W a . b . 2 . a Glutamine '6\ serine Y Alanine d Lysine e Arg '@ix c Ala d Asp e Arg-l*f3 *{)H kr 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 e. Place a spot of each sample on a silica plate and run thin layer chromatography 5. Post-translational processing ... a. Adds carbohydrates to Ser, Thr and Asn residues in proteins b, Adds the Signal Sequences that target proteins to the correct cellular location c. Could add a phosphoryl group to a Tyr residue d, A. B and C are all correct n ffi, Both A and C are correct 6. The two molecules at the right are ,d Diastereomers r' b., Configurational isomers \/ Epimers I- ' ( - 7 {t{ l " V.;, N,W\ 4$ Enantioers .W Conformational isomers onfiguration of {r*r-r I Rest of peptide f:.t;, l) Ju**r 8. Based on this graph, thi*gyggftuould likely... a. Bind an inhibitor that changes Vmax and not Km , filBind 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 F A Competitive Inhibitor ff A Non-Competitive lnhibitor J6il. n Mixed Inhibitor V en Uncompetitive Inhibitor *e. A Mechanism-based lnhibitor 10. The Y-intercepts of the lines on this graph indicate- K m- liKm- Km/Vmax The substrate concentration at which the enzyme is transforming Substrate into Product at half the maximal rate 'G) t/vmax \./ 11. Which type of bond stabirizes tfrfffuternafotructures of-gnill! an+/CeiiliAbe,lmaking them riE{? % '#F Y*ffi. c ($ Hydrogen bonds 5. Hydrophobic interactions t I. Peptide bonds ' {. Van der Waal's interactions e. Glycosidic linkages 12'Whichofthefo||owingisasignificantphysica|characteristic.@ a. Completely hydrophobic, explaining how it associates wiihlnffi675ne acyl chains Completely hydrophilic, explaining how it improves membrane fluidity by associating with the lipid polar head groups It is Amphoteric It is Amphipathic None of the above is a characteristic of cholesterol 13. Which of these def initions best describes a prosthetic qroup? ^ 4(mat part of an enzyme which OinOs ft+ Ouringpctcl-base catalysis " (!,) An organic molecule or a metal ion that is tightly bound to the enzyme protein jf A coenzyme or metal ion that is loosely bound to the enzyme protein d. An organic ion, or complex of organic or metalloorganic molecules that participates in catalysis e. Any molecule that increases lhe rate of catalysis without changing the equilibrium 7Z'N"/- l*"ryh 4'q t : i ; a....
View Full Document

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.

Page1 / 13

Fall 2005 Practice Exam Answers - ,tbt "--' '...

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon
Ask a homework question - tutors are online