Final (2008) - Universitny Hunslon ncus 3304 1-sz Exam...

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Unformatted text preview: Universitny Hunslon ncus 3304 1-sz Exam Insh'uctorDr. Briggs May 5, 2008 Name 7, , Answer all quesxzons, LAST,‘ FIRST Multiple shows 2 pm each (I no pts tom) 7 Choose me n :1 correct answer and rm 1: in on the Scanmm sheet Also circle your answer on Lhc exam and Shaw ALL Work 1). Calculate the 1:1 oflhe follow-mg peptide HIENVLysrPhchrp-GhrCOO— a 58 b. 94 9797 d‘ 1094 ‘ r ‘ ,‘ 3, None, his always positively charged. Q01“ T W“ ‘ I 9H 1‘1 'ozbicE—(fcx-irco; H co; My" CRHI‘I 702C—$7‘C’$C}11’COE H CO; ‘0“? ’OZC7‘C—Ly‘ cufico; 11 ca; 9“: '03C1c7$7c11yc03 H co; OHII I 1 ’ozcfi‘. J, cufcog H CO; 2 3) mini is the only compound that Can phasphoryldle the unphosphoq’latcd cmlyric hlsudme residue in plrosp‘noglycemc mimse (PUMP a. 27m b 3-90 c ways d. PEP fa) 75ml 4; 1n me cin ic acid cycle, cleclrons are tmnsierred from suecinem [0 FAD in which of die foilowmg “WV hydrogen alums b elecrrons are transferred direcuy 10 mm c, as a hydride 10D d esrnolecnlnroxygen e. as a phosphate gone 5), Which Cmy'me in flu; cilric acid cycle is allostcrically activated by ADP? n, (time synthasc (@nkemglnmele dehydrogele c. Fumaxase ’ firmich—nl Inc lalowlng enzymes i re onsinle mr the produc an al llie coy @Succinyl-CoA synilieusu b Aeonilsse c. lsociuam deludmacnase "d ‘Sueeinarc dehydin. misc 6 l-umxl’ase 7) Wlncl. ofthc {ullowmg dcscribcs the pl, or isoekcmt’poml? @e p“ nx which n pi-mem has a net charge ol zern h The concentralion of H+ inns m solnlicri c. The pH :11 which a prolein molecule is must soluble d. The negative lag of [11+] e. Tine log of l/[A] in" s' x) YOJLhaVe eieeled e niursirri f0 m of‘ V laced me camh‘fic Eiollnwiug ell‘ecls would you expect to obser’ve if’yofi alanine. a A decrease in the affinity for sunsnnre coupled [a a decrease in enzyme acii ry b An lncl’east in me rate of pcpude bond cleavagc due to an incrense in the raw of 30 phase camlySls c. An increase in me late nfpcplide bond cleavage due to en incre , catalysis (I A complcle loss nicnzymc activlty due to llie inability to bind subsrmic Nu errem or i. slight increase in Liffinlry for subsirnie cauplcd in 2| cnmpkle luss Cfenzyme the {me of covalent flelh'll} 9), Which mac {ouomng glymlysxs enzymes (5 NOT usch dunng glucnneogenes a. Aldolase /@Pyruva!€ kmuse mnose phasphat isomcmse 11' ansphoglyccmle mumse e Phosphuglucos: immense 10}, Th}; cgmmon dlsacchande {Jose cuntain: which of (he muomng monosauuhzmde women 4, glucose and galactose b. glucuse 3rd maimosc glucose and frucms: d gluméz onl) )A‘memse and gnlanosc 1 1) 1.. me pompcuuvc summon em enzyme, the mhibnor hmds mm enzymesubslralc Complex \fb mhihxzor bmds 111 me- meme binding pocket preventing suburate binding Mummy displaces the substrate from the euzymc-subsmltc complex to form an enzyme inhibitol complex d Inhtbuor reduce: the activation Free enelgy )Nonc orme above 11). Au omefouow} ggime acud mic Humming pnmcxpslc; in other flailng pnmwzys “ mcxmtle—‘# . wkmoglutmme c [unmmte o citraic e oxamacume 13) What .s the maxuunm number ol'molcs MATE man can be» produced from the aerobic breakdown nfnne male of gluCosc? a l b 2 NJ What Is Ihc pH M21 550 mM NaOH eomxionv (Sodmm hydroxide compictely dAssocmtcs m H20) 4 16.7 ' niliniued [l7 Lhe ho<fillalv Lnbmnwiy examinnliun reveals a very high serum acid. In addiiien lo taking steps in eel-rm Lha neides‘ Lhe amending physician prescribes Lhihnln’e‘ lhe rationalc for thiamine adminlsuation is ihsi ihiamine is convened in e menzyn » us‘ by which or lhe rellowmg relevant Enzymes? emit.- dchydmgenzse b, Pymynie ullrboxylasu e. pynivaie dullydrogennse il. Pynlvatc kinsse e. Tmnskemlese 15), What is ihe rsie or lhe carboxyl group mm is hem m [ha euhenyl of ensleseeme in ihe uiiric acid cycle? Be VERY specific, s. h is released as co2 via the enzyme eimne synihase I: ii is relmed as co2 via ihe enzyme py‘ruvnte dchydmgwase e. IL is mlcasEd as (:02 yin the enzyme wkcwglummte dchydrogcnasc It is released 2.; cos via the enzyme lsocirrzte dehydrogenn e. X! is mined in oxhloheeiaie for me hex: pass through the e ric neid eyele The diagmm mprcsums a “substraltt cycle" or “futile cycle“ in glheosc metahallsm Which of the following shimmean nheni lhe cycle is corrzcfl ly me MIL,7 l7] help esiahhsh an eqn ilniun. betwecrl new, ineialaoliies. Me: n ll produces ATP by snhsinne- level phasphory I nun. Fru-é-P Fru—l ,6-BF c Keaenon l slnlyzee by an hllosiene enzyme that is wind by fiuclosu rbbplmsphulc e Reachnn l is Involved in ihe biesynihesis ofglucosc liccik Am e Reheu'on ll ace-hrs under low-anclgv condition when ihe cell )8). Compuie ihe (3° for u reneiinn will. h KN or: 56 y lu‘. :719061 k. niel +19 kJ/mol c. +1906l H/mol d. s12 kllmul c. “2235 kJ/mol L_. m A nonapuptidc conmuing one or more 01 each arm {allowing amino ands, Arg, mu, um Leu, Lys. Met. m. and Val, was Subjected m we following degradatlve :cChmques resullmg m polypepude fragments wim the mdmmed amino acid campmsilions. What is (he amino Acid sequence ofme entire polypepnde? Note mm the dam below are NOT sequences but are Compositions!‘ I. Trypsm hydrolysis 1. mg ~ 2. Leu, Mel, m 1 am, He, Lys, Mal. Val 11. Cyanagen brnmidc neamm 4 Low 5 Lys, Mel, Phe s. ArgLQquUc, Mel Val a Val-II:-GIuerl-Lys-Phc-MelrLeurArg b. ArgvPlIc-MclrLcu-an-Ile-GIu-Mcliys c MngaH‘le-GlurMetrLeu~I.ys-Fhe-Mel d. Lys-Phc-Mcl-Arngn|~fle~Glu-Met-I,cu rngal-Ile-GlurMurLysrPhertt-Lcu y knnw'ias‘ g‘n iw HEW ("2.5m n ’ M m a salmon Containing acc‘ylchulineswrfls: and acelymmlme. The VW. and KM far mm =nzyrn: m 25 ”C are 245 MA and 0.4xxo‘ M, xeflaccxivcly. and me mm conccnlnhen was 2 5x! (TAM, Th1: Kl lo Ih HUN 7 5x10 M, Whm is (ht m Ill Velocity (Va) oflhi> inhibited mmm ’# "‘ a 0 0 W5 1: nm 1 M/s 54 \ 4.51 M/s d. 2H 3’ W3 0 21mm 1: r, O‘H CHchl 5 Y a,x=NAuH‘ b x NAD’ "" NADH’H‘ d» d.\'r\"M>+H’ e X \J\DFII H’ 22y Momma)"ch Edie” A“; .4, an» a A mold:sz um can form .1 hydmgcwbnnd yoer I) A mum-m: um In, (A nu charge 6% 3e —% 0J6: Fink (@A (new: that can map: a prawn u A momma what can mm; prawn :. A mnmme mm mm farm a hydmgnn-hund 23) How many nm are ikeru m n 321 m7 /. :21x10"nm M3 zlxvufimy [gm-M “mm @ n.32mo"nm a 32mm". moi“ c :2 mo‘nm WA 4 (w m PS 24; The emhulm' change ( \H) {or a manic" 15 r 7 s kJ/mol mm m: enn’apyclmngc ms} 15 55.0 unh‘mnl/K, Mm 'lhe free energy (m) for the mum m kJ/mo! ms ‘ :7 a 4x1 kJ/mRI—‘E h 755 ammo] c »57.4 kJ/mnr , , a ~xs.5m/mn| ' QM m m" / (\ . 7 an LUcmmcmcpanri sodium: mm 'lec pKuL)[ :1 jun [T4 21 ‘2‘: .ISBMW‘B L somnumomimng1min” D4\lnccnc MM m 1 m1 0“) 9M con: and 15d *5 ‘Z‘V . h .um'w'uy hm H mm Gm in: mnveéfed mm’ Lhmphuk: by FNZVMF. A and [hm L nvulml hum fmumserfirpho#phleu, an mrermcdimc pathway.hyphasphumanmn:hummus: Whu—‘h—T'mm' enmmyo , 'vw «'7 )‘mwue Km“ L» Huxnkums: c thphnfiucmkmmc a L a a Phwphnglz‘coic nomuv ‘ c Trvmuphosplmlcuumc 27) What tom mm; ammo mud cannot exist in the pHrange 1714? H H HerQrcoo. HZNr rcooH Mmkcrcoa CH / Si?” / A H rcoor NH,+r§rcooH gown gem / W / W 28) C' 4n: z szr 401 me 012 p1 of the amino and Arginine. a 9.97 b. 10 54 C9 10.94 d. 12.43 3 None, vtisalways positiver chugad, \ LL L W (Va MG) bS :0). Identify the singmcm ‘uqucncc oflhc [allowing decmpcpndc / \ sz Q \s \ o \O o \ 7; o HJN‘ N N NWJLN [ NJ N [ N\(KN (N ‘o’ o 0 CH1 0 k 0 CH, 0 \OH \ coo» a. FTNALDTAMS b. New. AMS g; mum av FINALEWAMS 31). mm parcmllage mm )‘usudme imidmlc is pmmnaled at pH a 87 / 100.0% K} 17.95% a 1,4 m :1. 5,75% 9 10% u>xr ‘ __—A—— 32). GIVE" Rh: uflklnn mud sequancc F’AGTKMDAWGH, What reflgcnl will cut this pcpllds‘ ink) two equal length pieces? an, Trypsin b Pbenyl lsothincyanalc u Cyauogcn bmmd: ‘ A 9 Chyryojrypsin ,, 59 w M» ‘93 ' ' : Indnncemc \ M ‘O’QM 7’ V 3]) Wu '5 the (owl: aucngth, 1, u a so mM :oluuan creaswonzv V JsomM # W "L b ASan , ‘ flsa mM E 90vale e A300mM 1/) h 34) The a) dihedral nngie are pepiidc bond i< described by rouuon abam me bond 21. um is between [ht N and L atoms. h that is between me Can and CB mm: mm is bow/ten fivg/szud}; items, d, mm is between [lie Ca and c atoms e none nmie abnve 35) SDSVPAGI: is g a a dehydranng gel technique. L (fie denmnnng gel ftChmqu: ’L = c an anaerobic gel ieehniquc / d. nhydmphziic gel technique S$773 *' Lg e. none oflhc above 35) What is the fractional Saturation ofhemogobm (“93153.3 10er Assumc (hmrFS and rim Lhe Lg ofhcmoeiobm i: 26 ten for “us calculation 26 a: /_._r_‘ i 4‘ 37) Affinity ehmmeibgnphy is used to scpamte protein: by a SM: n mas: e sallinguut ,q. saitingin L’ejigand binding 3X) Given me folkwmg 4) and u angles. what is ihe smoudm’y ennciurc m whicl’u’iins {undue is involved? 7 <3 '5 Phi(b, deg) rsiw, deg) 74 e140 140 /éx * 8% 3 Alpha help. (ngm handed) @Anlkparallclbetaimnds , , e Alpha helix (Ien handed) d Parflle‘hetasunnd: e, Collagcn coil 39). Ln what nine. \Anuid you mm the nnino neids Gin, Lys, and Phi in be eluted earbuxymcihyi column at pH 72/ e (ilu, I‘ha, Ly: Fly Pha Glu ‘c/1ine,L, .Glu d pne, (win, Lys e Gin. Lye, Pm» 46}. 'What specific portion of the lgG antibody is responsible for binding directly with antigens? a. Light chain. b. Constant region. c. Variable region. d. Heavy chain. :9-lyperyariable loops. 4 1}. Fully identify the subunit composition of a protein fi'ont the following information. Moiecalar mass by gel filtration: 35!} kD Molecular mass by SDS-PAGE: Elli} H) and Iii] kl] Molecular mass by SDS-PAGE with 2~mercaptoetbanoh {GI} RD, ED RD. and m kl) -S-S- is a disulfide bond and I H] are non-covalent associations fill 1' "'1 £517} a._ w5~S-lfll}}[8i}-S-S~Tfl] - (3&1, .53 "E. [lflfl-SG—Sfljilflfl-S-S—Tfl] _e.—- [tons-s-toos-tojlso] ,Mtoo-s-snoo—s—somo; Filflfl-S—S—lflflaS‘Tfl-S-S-Efl] 42}. What is the identity of the catalytic triad in serine proteases'? Asp-Tyr—Ser AspHis-E‘rer 5;: one: a. 5(1 Ha: W /c( Arg-Trp-Ser 43}. The lines on a Lineweaver-Bnrlr plot for a mixed inhibitor, with the variation of o. and of (Le. =1 .o, 1.5, so, etc.) are characteristicain w a. Parailel _ Perpendicular Coincident on the lefi of the Y-axis d. Antiparailei e. Approaching V,” in an asymptotic fashion 44}. What is the half-life of a first order reaction [th with a rate constant of 56.16 x lii‘1 see"? a. D.fl1234 see b. D. i 134 see c. 12.34: sec @iasnsee _, o. :234n sec L's-5 : IGfiE/nglgxig'q :. 12%733‘11 iii 451. What is the half-life ofe second order reoetioo {to-,1 with e rote eoeeomi of 1.155 s is" We" and an initial substrate eeneentmtion oflfll ti :1: iii‘2 M? e. 0411234 see b. fl+l234 see I e. 12.34216 iH d. [23.4see * - - - if‘-‘‘»"3“*"i=""Y‘ihineiino“ _i_,,...'_-—-'-'—" 01234 U see 3 it e = $1 #5}. At what concentration ef'S [expressed as a multiple of KM] will v9 = {Li-'5 Vmu? k .._ it) E. KM h. 0.3311“ U0 -: \JWX CS3 e. 035 KM fiigfi: Vim + [glee : TEES-l r- A . 4.. Pi; i7$UMYMw J‘ Sviuovihq :i. f L J ‘ [Kiwi visa—5:533 - 4?}. What is the name of the enzyme in the glyeelysis grams-«vatsr that is responsible for converting 3r phespheglyeerate tn 2-phesphe liberate? - a. phevspheglyeerate muting ' QC)“ H" '1‘ ‘ 1 ‘5 ‘3 : LIB-.1 h. triese phosphate isurnerase ._ "'31 hexeltinnse " if. pheephoglyeerate kinase e. fruetese~ 1 ,fi-bisphesphatase 43). For a MiehoeiieMeoioo reoetion, ii. = 2.5eiii‘iir'e“, It -1 = 411025", and k1 = fixlflzs'l. Ceieotoie K“ for this reaction. “ ‘—_——# . 6.5M $4.0M e. lflht e. 0.5M "95-! VICE-{fl k30?\ eerie _ ___ '2 we WSW 4f il 49). Compute Lhc {rec encrgy for Lha overall reaction beluw LBng the halfreactions near the and of the mm ATP 1 Fructose + P1 -. mama—1,54: + ADP + H20 71. a 11mm h 1.4 kJ/mol 2/013 c. 7 57k1/mo1 13 s kh’mol * OH: c. 1 46LOU/mul ATW ‘ *% 24 Di 5 H10 30S Fruc¥b$¢+ P, —% F/u Hwy/M 17 HLO [‘8 WWW” ’>F’“”?“"g*0+‘+@ («,7 (SK ATP,+P,— 7‘ Am: +1110 maxi 1 (>1 : ' 17. 1775110“ 0. 2mm“ 15911107 7 r ,, e. 4606 v U934 ' EL‘E‘Défiés (.mb’sl'fl C smdam free magic: (AGV moI) )ofsomc hydrolysis and phmsphamlysls reacuons. (R = 3.3 mm 0'3 we Rmcmnu Pruducu mum/man 7 P, + Glucase Glucasc-S-P + mo ATP + H20 AMP + {in _ Glues»! -P '7 mo Glucose +1). Glucusc + p. GIucaseJ-P “1,0 1.3-1Ephosphogl mm + mo = msphasphoul mate + P. 7 Acetate w. Acctylghosphale + H20 Phosphocmatin: + H10 Cmatine + P, Hzo 4» pa = m V chtasbl»? Y’ “10 Frucmse + P‘ chtoSc-l.6-P + [-170 meoseérl’ + P. Acetyl-CoA + H20 Aztlan: + CoA w R ‘ O\ \ ...
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Final (2008) - Universitny Hunslon ncus 3304 1-sz Exam...

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