key_mid_2_winter_2006_mwf - 10f2 BIS 102 Name'3 Winter 2006...

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Unformatted text preview: 10f2 BIS 102 Name ['3 Winter, 2006 MWF L t F as irst K. Hilt Second Midterm Score (100): 1. A pentapeptide is subjected to acid catalyzed hydrolysis and the amino acid residues separated and identified as we discussed in class, using an ion exchange column and a step elution of pH 3, 4, and 5 citrate buffers. (10 pts.) a) Let’s assume that each amino acid residue in the original, intact pentapeptide was difi‘erent. How many peaks would you expect to see? If there is more than one possible answer, then give them all and explain why they are possible (i.e. give the chemical basis for the results). €055R101\\-\\‘e.s : \3 '5' (gem ;£- 5 Aim aha”: H \ ‘ + a 13 a 9“)» <4: w:— «a C: Q or “K semi +~x 3) mwtfik—AEE—Eis—E ——=. H 9W1 E,D,GI+NW~T D e 4- \ ft“ *‘D 44L “RH iM. Ann/731:4 {A 53k ohmiu5 "1~ Q q. p break, J‘wd' 151m, KWR‘L” 1am. +1 (5 pts.) How is each eluted amino acid peak detected and identified? Give the complete procedure. List all chemicals and equipment needed. 4- z +| 1) Niniijm‘“ + 4.0.. + M a» ecu—Lav (see—WQWWX 7,) iAMr‘nf-ie3‘ Mac) 5+MMJ~4 *1 2. A sample of the same intact pentapeptide discussed in question #1 above is now subjected to amino acid sequencing using the protein sequenator. (20 pts.) a) How is the column chromatography in this procedure the same or different than that utilized in question #1? Give a detailed analysis of the entire chromatography procedure, including types of interactions, resin used, elution methods, detection methods, analysis of peaks; etc. , m RAMA“ M24. 0»qu \«DMQMODK: *EWWHW‘ We“ Wm kb‘ : :0. I': My. ijJ-Va‘okobt‘g inbrntfim . +2- 2. (km M is C';3¢9~u¢1 507°“ beak. Eiwi'l‘m is We. on arabc’d‘ +2. 0'“- Mamic solvw. ELHQRM i$ 1m) $e¢dwoek¢ibmirj (A261). cMmmJu’s Mim'i'b 4—4.. P “a “punts PT «sirw. (5 pts.) b) How is the data printout fi'om this procedure the same or different from the printout in question #1? Explain, by comparing the chemistry of each situation (question #1 vs. question #2), why these two printouts should be the same or different. , +2. Di‘trf'orovd't‘ EMA “TL. :» Mm *2 366% m— gmfk emea W1: m XQ$¥MW is Aha-o. +0 HM. 54mm reaayat chmhflj a. wad“; a\imiv\a\'\‘m 01 SM: 'Hn-t. N’WMinni and. in Wlm*2, 4”- 20f2 BIS 102 Name E44? 3. (15 pts.) How is this diagram related to the reversible binding of oxygen in hemoglobin? Give a lengthy explanagr,&5t ties in this diagram to the overall mechanics of this protein,3at the molecular level. 4—1 1i i .1. m MASTLM (WW1,th ’9‘“ Fear; :w M w 64t- W 0". We. \'\'\0 subuni‘l'fi. BMMj 04‘, 02. +0 ‘HM/‘L Fe‘""l \ 3 ”Win? €¢+z *0 new W ‘mh thu. QM ’4‘» HA"- Q"?‘"‘Q"" W Tim??? As M “Fe/*7" (WW, inb m "M. i“ bv‘mcbnrm . +2. \ \ evosu‘MJe W‘s-HM WNW 1*. M *“W’S 0» MW in W OL'W' MHz/la» break/1v 51M bvhkafiafa 4. (5 pts.) Would the pKa of a histidine side chain go up or down if an aspartate residue in the protein, which was initially close to the histidine, moved away? Defend your answer. it mus-56%) mm D“ w» eke-:4. -\’o H ‘ H wag. («Leave ‘ i 5n) w “u. m Pt“. 4mm. MW 5' Lean“ | m H0 $07M r5 W¢¢& ' ‘41 a1. +LIL vo-l-M . W‘ Kg. AA. H +H€5 +0 4301* U Q LR’IT‘J wt #1»! mMunvln‘M 5. (10 pts.) List all of the various types of secondary protein structure that could be found in a protein. What do each of these structures have in common? Which structure is most likely to have a proline §n it? Why? “/WH' p,€|eam 5km! ’l'l 4' «v», (‘Wé—L ‘l'WM(‘5-M. Moll H— ’ MM... M a4 MM H'MMJATL «Wu, MW MM 0. 9H? , l—WM L new kink ‘m M 5+Vuciwre.+2 6. (10 pts.) Chaperonins are protein folding chambers. We discussed in class the folding chamber found in E. coli. What do these chambers “do”? Describe in detail how they accOmplish this. Do" '1: V) (youth. a» spy. have“ 30’ vefiulhna “’ z) WES. Hm. Qwfl-eln \9‘3 ovov‘xéclvuj a. kjgquft'c \Hru‘n‘}. *1 AowMfibk m 7. Clad MV;¢OHW*£W:_ C ll: II W * ‘€A’3 M&. “— M4— 6"" l A “"33 LAT?) 5m amap "Ha. neweolw (JAM-1414’ \iw‘vw) +9 co‘M, \r'e‘tuau'wg 3H»:— gop‘lflh 5° ‘HM-x 3+ cam flail-:- ‘0‘. 7. (20 pts.) Hemoglobin has numerous allosteric effectors. List all of them (exclude CO) and indicate precisely where each binds. \\ 4" 0:. W *L *1 *1. . H H" cvwm‘tnog. H a", B’fiwlowni‘l’} + N’Jumirnfl “"2, We. til—submits H 00; M—+wwm.l Niki an"? at .u “l Mums +3 «4 +1 396 cth ww‘i"; . ‘+"<)mma.u m p-wtumrs *1 H C\’ bdm R+ m ma. 4-5ubwni‘l' MX N-va‘nag NEE;- ’1‘ W u-5w\om;+ +3 °‘\ ——————————mt3+ +_9'- calms;— ...
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