BIS102 Hilt F06 MT2 KEY

BIS102 Hilt F06 MT2 KEY - 2.. 6 ‘ ' 1 of2 BIS 102 Nmeu...

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Unformatted text preview: 2.. 6 ‘ ' 1 of2 BIS 102 Nmeu Fall, 2006 Last First K. Hilt Second Midterm Score (100): . ( 25 pts.) Hemoglobin has three different histidine residues that play different roles in the reversible 2 inding of oxygen. One of them is the distal histidine. What are the other two? What are their roles (if there /-\ h 1"” v ' more than one role, then give them all)? Then rank these histidines in order of importance Ge. #1 is the at? ' ost important in the process of reversibly binding oxygen, etc.). Then explain why you ranked them that w 33" f , a i l h‘ “MI” . faith 1‘ 0 «No.9 The same OLIWW" {her cars is the “WW ‘9 “5/ l 5 P l9 3 Ctmd‘l finiali-roal his-Howie:er Profimal hairline, \m‘ absesf +0 heme geuttr'mtml’wfilhfllf is covalemlhs bended +6 tie Fe” @ adistameog 033$ iePWIWi hl‘il'ifilll/le we 4; am “mm,” (our to keep The heme inside-the AWN” {htervbr hf Ha Hb subunitmot [ways Hie, Fe“ M a “imam orientation to Air-he prat'opov rho 1,30 that Olcan bind on +144: m her side bed—1w mean/hi pkiS'l’fll hkgtsol}n€.Th€,m-fnl [his-Hdl r0 a Y‘Ole MO; is flqe/ “we of 1.142 B‘Subu M the {framth We? wcl’x P°lfil°£PHdechain.Tl\ie is bivalve in The acsdic 30hr Writer? whirl: kaes 7mm haltle {0" Q; to binol r rhe'hexwt’; as a r€6ul+ (rt; +hf;\nega+h/e he+€ro+mloka§jlyf Wt. aim-r Hort cow's as a regal-1; 04am Covmaflm of; a sol-t bridgewiet" 995. l g C ‘ 'Ml ‘ “ ‘ ' omm-in lei ; our ' M liq-WWW“A “gimme allialhflaindkgulgngrgmmfiumsl iLnb/bm—vvhe heme-fwmlggif: £4:th 1513(6de l‘i'mdme C I wmlol hug no we +0 hind ‘r‘b hfime care/CH5 become 1+ vuon may ~ n2 “Ll—lac Ti onmtwm‘dam {sabnm' mart- Important because Wfkowt— i+ (SM/“(4 M ' (>591, back page mat as well as a maul-r 0-? HM [05:5 09 “*5 H'bm’ll “3 Oé- H44; 'A 5 (east iWyaar'tam for role, a? ‘/ becausealtho‘kgl‘ l4" MIPS lfl‘H’W \ Jl‘l’f'mbog'h “try:- Hle/nz arzrvsot'her Hamil“? Mend His) kewwt'varnc «(tavern dreams Hm 5 am also net,» wtfk +l’mr. +3 2. ( 25 pts.) The Sanger method and the Edman method are both excellent ways of labeling and @ identifying the N—terminal amino acid in a peptide sequence. Let’s imagine that we are back in the 1970’s, 2. - ing these two methods by hand (i.e. the protein sequenator has not been invented yet). What are the ilarities and differences between these two techniques? Give a detailed discussion that shows that you ow the chemicals, procedures, and concepts necessary to carry out the analysis of the N-terminal residue using both methods. Which method, Sanger or Edman, is better? Why? I The Gin/Mi luring; oLal-ae, 4 we «ramming owe Al’qu beH—k use/WW 0‘? nucleo. lx\ic oft ‘h v ’04 w ‘4‘ t. - — ~- - ~ I r p \ <1 “C 31 o: “rennin ammogroupfihme y wgl «my» 0N uwtwi m [dwtuafbms fiemmo would «If-the Ne+wmmulemlwirh later amigcsigBo-rh alga wee/mire analgsies‘F av3€{flt€41+‘{¥a3m9flt$lm otuervww ms +he segments, in , Til/12 (Kt-Kemw are, flamerows. (danger o Ulcmqicmfif reagefl't 0;” F (lawn Edman A’ ( Vii/:5) Swami; marked regnzres email pepfide {insane/n+5 (~3oa’s Ema/Wham; 24mm '5 marked alibi {or large, 4m5men+s (~49 aa's).§av\69r wseoi out‘+i'n31wl; NH «.15 CNBI‘ ngsin, Mot mflwwyaén matte We, arm‘s), wlm'le Edman wsaoi arcs/C, e-rc. “Banger Meal or DlvP—m. analgsis WSEtAS TLC redrwkiek DNPvunlt.mu-m haul been eluted. Holman. Mai HPLC am A5933; To det'Q-V‘M‘M- W [0" ?TH' om» Md been elected, fl 9 l i r *‘ ram/toms Mtxbocl ‘9 louder became larger \Cra'SVnWltS CM bfi “Mlgn’l/ WIND“ V9 [95$ Waitms lama! twgmws. Batman’s method pulp-fans +‘l/hfl 9 at; W‘lflélfl‘ ?l\ (m3 x “V -/‘\\‘\,I 6°49» We «Courts-{e atvwi can we ,t E ( “56 lawyer: 20f2 BIS 102 Nam Name* 3. A histidine residue in a protein has a pKa of 6.30, when the protein is in a buffer at pH 6.00. When the protein binds molecule “Z”, the protein changes its conformation, causing the histidine to become a better base. The histidine side chain is now spending 20% more of its time in the protonated form. owbgi Lib ( 15 pts.) a) What is the newmpKa of the histidine residue? Show all calculations. Recall that Ka = xz/y- @ x H = pKa + log {[b]/[a]} , p1 = (pKal + pKa2)/2 , and F = q1q2/(t-zr2). - Pazplla*l°si§:j)“ b:o.67yeé>%£4 PH: Pk‘+l°3%7> J W ‘ . , om ow eoo=6ao+logkfl+l Ckil’o.qr750% 6'00 loam; qu Jr; ~09: “05 2 (29;: “a - 7, t a,“ l. _, .7 ~ b ' i0 pts.) b) Indicate three different environmental changes that could have resulted in the above change in the histidine pKa (i.e. a particular residue moves close; a particular residue m ves awag ,etc.).‘ W W The ecu/no polgpefiflvle, chain W‘s-Wheoause “PM sawr ‘3 c inaer that/“i=5 much weaker (a: +003). Pr CZ' wombat kl '655 like“ +6 Vitamin a all" ridge lee-tween ireélmc anal The H|%,siflce ‘rr twat, fosijévz. Lag-tit) Hi would no“f 30 Hz Ha, Hiefldine became: the pl!ng ~Q “L5 a ’0 I“ 4. It is possible to gently remove the subunits of hemoglobin from each other, without destroying the biological function of the subunits. When this is done, the a—subunits remain independent (separate) fiom each other. Their oxygen binding curve turns out to be similar to that of myoglobin. The B—subunits, however, spontaneously form tetramers. Their oxygen binding curve turns out to be similar to myoglobin’s, too. /\ ¢ ) (10 pts.) a) How would you gently remove the subunits of hemoglobin from each other? What would l I ,‘ ou add and/or do to a solution of hemoglobin molecules to make them come apart, without ruining their " biological fimction? Why does your method work? Why is this process “tricky”? To get/1W5 remove, Hm smbwl‘tfi 30V» Wombat «dot excess amouwfs (31:04 so m we album-:5 wi It be, i V“ ‘t heir mm"? min $84 150W“ . Tlfl is 01056 tit Y‘ui Vt+hei r‘ balm/mt [we a Tita‘f'c wl'wt rhea thxh gap. 0 ‘ m ( 5 pts.) b) Now that the subunits are apart, how do you physically separate the (Jr-subunits from the imp-subunits? Why does your method work? LTD separate wrhe (X Lrom {3, \flew would add EPG since 0"“3 B'gai’ou‘mW bond \ (3 net \,'\;\“\(_’U WU; Likfl 3th..“‘_, |\9\3'\' o-Smcix Cxit'w‘axkfw' w/ PG Jr .X B (7 / (Tale cw’mm Via-23¢ wt ‘v)u&')\,:\\i"\ (U t9? '{C‘ (4’) (.17 g ( 10 pts.) c) What do the results of the oxygen binding data for the separated subunits tell you about the normal functioning of intact hemoglobin? Explain. / A» “Y [0 v V . hes-é: mews sh ~ rm Hlo wail-:5 “t new it: ha i be: $23 '* 5 a A , I t .1 r . Swahiigye ,WWd/x we :WSJOVWW' Mfié‘f warmed-356 lowlime :9. a";,Tl\cse f‘i’uiggg Sela wits rel/‘1)? 9%9h_,,,,Qt£1er wok Co mmumtate so that? 5’15 if); “t "i <5 wxi’x \Jvk“ \\, \fl. \, Ow that as am :1) W? W gable . XMétiOmr y 33M xvi—5i C'Qmmkugtfidav}, 'l it“); Ox pcth-JMKA efc ,‘EWQC/YUFC at resent e I ‘Ir-t’ ...
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This note was uploaded on 01/31/2012 for the course BIS 102 taught by Professor Hilt during the Spring '08 term at UC Davis.

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BIS102 Hilt F06 MT2 KEY - 2.. 6 ‘ ' 1 of2 BIS 102 Nmeu...

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