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bmb3100-19980806-THU - fig BCI-I/BIO 310 FINAL EXAMINATION...

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Unformatted text preview: fig BCI-I/BIO 310 FINAL EXAMINATION Thursday, August 6, 1998 l .(6) What non-covalent interactions are affected by the solvent, water and how are they affected and why? H LAWJC — Wfl/umix lit/VI 091% It M J7" mag... M W 4W “3 ~ 17 ( 41;.[71' n/JA(Z::/ W4$szdfflmt [tar/x- 79/56 L45, 49,67— waltz/3:16 i145}. I.- tau/1 é?(¢(gsAI/ifj//f/4H"1A” 2.(20) Match: a. secondary structure _C_subunit molecular weight b. hydrogen bonding isteric complementarily c. SDS—gel electrophoresis _f_serine protease d. transition state stabilization __cleavage at M e. van der Waal’s interactions 3: proteinfpeptide sequencing r. trypsin 61 J l:__ a. helixffl sheet g. Edman degradation _h_net macromolecular charge h. ion exchange chromatography L‘bxyanion hole” (chymotrypsin) 1. molecular sieve chromatography _binding site j.. ammonium sulfate I average macromolecular size Q.) Emsyl tRNA synthetase 425% 1. ix 3.(6) Draw the binding curves of myoglobin and hemoglobin for their physiological ligand. What i_s th_e ligand? 3-0 A! 3‘ A 3,1167" 1‘ Q finial-‘1'. €1.53 ' 0; (I) flu: lxjm‘cl. 4(5) Draw a Lineweaver-Burk graph showing noncompetitive inhibition. Label the axes and show which line is obtained in the presence of the inhibitor (+I). 5.(4) Draw the structure of ascorbic acid. 6.(1) What is its common name? - J” (”1121/14/«4 C 1(1) What disease is its absence associated with in humans? MAJ/L a2] 8.(4) Given the reaction: ubiquinone + NADH .- NAD+ + H" + reduced ubiquinone Calculate a value of AE°', volts, for this reaction. See table on next page. LL!) iffif'inolflé' 4—2144 +291 ___:_) (Eff-L 004 IJAW +2H74iauw-9 UADH 4-H? --0‘3‘;L 9(1) Is thisaspontaneous reactionaswritten, or not? {E’w’lL-{fiia rat. J”._ "‘5 Jr“ 2"” ' . .,_ A43 ”mg, 5? 3-24:}[0déj 3032.. (A412:- lb “fit-if) {5‘ Mjaiidfi 0.01} - 6‘6 Z 4: fl" (xi/midri- :5 flag—— " "r J H) _ 00 O 56 Jo {7:5 ail-ES \..—L-""“ - ado 917; Fr” V99": 1 M I} .. a 0‘5 2. mré‘frxri x 0.04 $0.32,] ,-; O. 3630 if; Table 11-4 Standard reduction pottntlals for some important biologiul half-reactions H Reduction half-reaction E" (V) -——————-———_______________*_ AcetleoA + C0, + H3 + 2:9 —r Pymvm 1- cm -0.40 Femdoxin (spinach). Fe®+ :9 ——» Fe® —0.43 2H6 + 2:9 —. H, -o.42 a-Kelogluuru: + C0: + 2H0 + 2.9 —> twain-m —0Ja Lipoyldehydmgenne (FAD) + 2H0 + 2:9 -~-) Lipoyldehydmgemse (mam) -0.34 more) + 2116 + 2:9 ——» mum + H9 —0.32 mane + 2H9 + 2.9 —+ NADH + H9 —0.32 upoameu + 2116 + 2:9 —-—» Dihydmlipoic acid —0.29 ammunn + 21169 + 2:9 -—-> 2Glumhione (reduced) -0.23 Fun + 21169 + 2:9 ——» FADl-l, -0.22 M+2H®+2e€ —+ W, —0.22 Amaldehyda + 2H9 + 2:9 -—» 50ml -0.20 mm+m®+2e9 —» Lamas —0.1a (ix-lemme + 2H0 + 2:9 —> mm " —0.n leuomcb,(rnjczmomll).Fe®+ :9 -—» Fe® 0.02 Humu+2H®+229 -—i Such-me 0.03 U'biquinone[Q) + 2119 + 2.9 —-» QH, 0.04 Cnochnrneb(mitochondrill).Fe®+ :9 -—» 12:93 0.0a .L‘ymcl'n'm c..Fe®+ :9 H Fe‘3 0.22 ;_Cynochmmc.Fe®+ :9 —-> Fe® 0.23 'Cruhrorne a. Fe® + :9 -—> Fe® 0.29 cmmy. Fe®+ :6 ——) MB 0.35 1409+ 2mm 2:9 ——> N019+ 14,0 0.42 mum 9700 0.43 Fe®+ :9 —-. Fe® 0.?7 I001+ 2H®+ 2:9 -—s H10 032 ——————._________fi 10(8) Draw the Haworth structures of two different ring forms of D-fructofilranose and D- galactOpyranose. P " \ r1 " '3' 1/ \‘g‘ l .- ‘f. l. >5 ' y .‘E l . 1 T T" 1- 3‘: I4 (H I 1. [iii 1 \ _.‘--- (u. '. f .r. . \ ‘: . = 'h, N. if'i ’ \ , 1 I /, i. 1 1.(10)What bonds hold the two molecules together: a) glycosidic b) ester 0) anhydride d) hydrogen e) peptide. ,- . A pyrimidine to ribose in a nucleic acid .-C E/ . Adenosine to phosphate in a nucleotide [2 . . Alanine to arginine in a peptide 8 . Glucose to fi-uctose 1n sucrose 552/ Sen'ne to the phosphate of a phospholipid é . Glycerol to a fatty acid' 1n glycerides é One peptide chain to another 4': An amino acid to AMP 1n amino acyl adenylate 4Q . Th.e complimentary bases 1n double stranded DNA Q . 0 An amino acid to a tRNA 5 La 12(8) Briefly describe the pentose phosphate pathway and indicate three functions of this pathway. a. _- . , . __ _ _. ' - d/ngppt—g' . . , I! _ .. , . .-; \ .- /./‘J '1 _," --:x' ' ’ " ‘x’J’ '-’"/-.-~ " ' -/’_' 1" a -‘//fi " r 1" / / (K \ f I _ f ‘ I (- - / ’ f/' r . —’ / //J'(’q- — ,r r fl ' / 2' ffi;_ ‘ . ,/ x "/ ’ , /’ - / — .i \ ’ a“ f I “I if //1 ,A-\ I {ll elf/fl; L X ‘1‘", i ' rl/ ) x; P ’ “ -. // 1/ r f . I / ‘ / ; x "/ - 1" r 7 f, . L/ A / '9’ ..//\ , fi/ , . ’ ‘ / . _, X . i - g f _.( y i, -" — ; i ‘ _/ / ” ‘ ,J f" - r“ til“, /' t I A ‘ x . , __. 13(8) Write the complete reactions of enzymes which form 3 NADH’s and FADH2 in the citric acid cycle. I j a l ./ a * t ' ’ II I ‘ “ .f/I 7’— II / t — ' / " - ’ F — - .I f u. 5” x .' " , ' t ’ x I {I K 5 1 I K .« ‘ _ ‘ [2| _ r 7/. 4/ _ ‘ __ I , i _‘ f I / r / _ ' 3‘ I"! / r" - a n, _. , / In 5 .. / \ / I .. .' . -. x _, r / , ,- (f y (1 _ l? A = \ Hf ‘.. F / ‘— J , 14(8) Describe the unique role of ubiquinone in the electron transport system. Be sure to include one and two electron carriers in your description. How many moles of ATP are formed when AcetylSCoA is oxidized to 2C0; in the tricarboxylic acid cycle and the resulting reduced coenzymes transfer their electrons to oxygen in the electron transport system? at» i /: a v 5, ~ “ / , ~ : A; J r . .. r l I .II ._ _} j; 5- __ j d) :3 3 _ .L') -7C. x:- _. 15.(10) Match the following enzymes or components with their pathway. ; LB-ketoacyl ACP reductase ,, LIE-oxidation LMalonyl SCoA a. Fatty acid oxidation Lacetyl transacetylase b. Fatty acid synthesis . L B-ketothiolase 0. Electron transport chain r_r_'-_citrate lyase (1. None of these processes LB-keto ACP synthetase L Ubiquinone , LL-D-hydroxyacyl CoA dehydrogenase A: acyl carrier proteins 16(6) Write a sequence of reactions which will convert acetyl SACP and malonyl SACP to the 4 carbon acid, CH3CH2CH2CSACP and C02. n O \f" i ;.- x .1 f 2 I fj r x v f“) :5." I {r V 1’3 4 fir/.2] J , I (1" S. ‘ , g ’ II, - (/‘n‘ .- II. (If/5‘63}, L \ ",’ Ar; .{gfl- ‘ T‘ ’— r~ 6* H» n : i -' e x :I I‘ ‘7 * “ t“ H 5 W \‘I 1'. PW! ' ‘t r ' 9 11(6) Write the sequence of reactions involved in the oxidation of CH3CH2CH2C-S-C0A to two moles of CH3 CSCoA. n O O- n /'\ ' C‘ CH5 ml L-.-./-/; s ,4 {/AD \—> FAD/r14“ Lin/Al. if}?! ?' ‘- (Ir/ti“ 4" ~. .- - x- .1; J a-MH 0H W .. r /‘ _._ ,4 f“ "T _. #3 CH 0H; (.5. ,4 / cw“ J H 9 AM 0 H (3 ’f 18(6) Write the reactions catalyzed by acetyl CoA carboxylase and B-ketoacyl ACP synthetase during fatty acid synthesis. . “f - ’ ' -. ‘ ' ,z' " I PI ”I .3 o Ag [[1, ;_ 5 (1., I + {’Q 74 ,4 / w w? //’/a [m 5’ __ JQA +4 4 7* Q //C{ %;/6 SAC/D + I") /a_/0 ’4 ‘ {/(HK/It/i/j .._—> 1-73" 1/ Y:(’\ n fr, "(I Ir.""v..i’![ “frag”, .Pi/z .. x ' 6 L." _/ [Kara/J L,.../ “s? 19(6) Describe the reactions which form triacylglycerol and phospholipid from CH3(CH2)HCSC0A, glycerol phosphate, choline, CTP and ATP. ,3 1 . i' ~ , g ’* ’Jp/ .ir / / flizf’ ‘- A / t x 2' /’ ’ ’ f " _. r fl "” /- ‘ ‘ 3/ 1: "Je , .7 fit: I 1:11 ..-, 1‘ ' ' rr ,2; ‘ _ : .r’l {4/1 J'C (Wed H ”IL ”.L r - ‘ ‘ at ' m" I .1 —fl— 7 j A" )1! I F; *‘l w? I- " f ‘ _-\ I .. , 4 _. L F ., g 3 “4.. l + C“ r , , . - e - . , -~ . An" .4 " \K V * aw , e - , — 1'; 4 .’“ i251 .i ' - .r' + r 1 [ ._ / ‘ 1' I' _fv,/1 |I JI ... Ii ( f; t L L" ‘- l 5‘ { ' ' ' . 'lr -: L . | "a: x. ‘ A {1 MI in): nu. 20.(6)a. Write the reactions and describe the role of citrate lyase and citrate synthetase in fatty acid synthesis. What are the subcellular localizations of these enzymes? b. Write the reactions catalyzed by acetyl transacylase and malonyl transacylase. m l "XC‘tL/lrft"! ”5‘7; rill; 4-" CH 4 5’1..n. , "vi i,‘.».:"1'*l:— --l 5.9”! j..!__ 4:4 ”I i“ 3 I, l I I " I'T'Tcif'; \_ . I? : )Jy-i lf'C/E f9 Ig‘irl‘r’t’f/t % j \l" , A t ‘ 4': avail/{twisty ski/“u“ii-Qt a - ”l i f L _ 5| . __ y n 5/1“ f/SQ t ' J ‘“ ; _, : 4 I» r , ”I! , 3,", J. ‘_ \(tlng’; , fl/ 2 2' -, T ‘. ' __ . I _ _ , / _'_ __ .. .l I: , _ . . {I ’ Jz/7(‘T{r- :/ :f ”(If _/,‘ llf' ll / / Ll." ffl/fi/Il/ E? .:--} ._,I _' k: _.r -".f/ ' ‘ fi/" .4? .0 r ' 'd I! ”a ." - 'J/ L. . - ." ' _/' r' r' . . r . I _' I. _ __r / " ‘ lj/j ’ \ . ' ‘J'z _ ’Fl 2'1 ' fl; ’ I ,-" ,- ‘. f/ I, _/ _ diff/IL J: 4.. _/( /) :. _ i/.' i ,.x 1. ,_.;/ /'/‘/ 21.(8) Briefly diagram the replication fork and indicate which DNA strand is synthesized continuously and discontinuously. Be sure to indicate the 3' and 5' end of daughter strands and the proteins or enzymes involved in forming and stabilizing this structure. _ {(tflL/ff."./? .-i'[.. .’ .fl- (dbl/'3‘” (’3 4 ,‘II . f I I r - I '/ -—'——_ I I I'. _ 4’ , . ‘ , .. r_- .-—'\ - .4 \VII .ryL/Jggu 3': I id ‘I I I \ f ' r. F' . r. l- . -...-.-.__, ./‘-.\ ‘ f 1‘- Il- '. I'll 4| I. i- 2 l : lg /' ./ i. O . ' I .‘ Y \_-_ ----- 3‘ ‘ lap-r.— 2/? I. I r- H— ’1 I-‘u—l—— I #f‘ l i f r K N. ‘ . I fl (Al I . f ‘ A x 1': rl‘ ll ' ‘ " . _ r n “r f f t . Ill ’ __ .. -’; . _ .. , .I . if I. - __ _./\ f X' _. 'r f. I {f5 ~ ~. .r- '4‘“ 22(6) Briefly describe the reactions catalyzed by DNA directed RNA polymerases. Discuss the specificity of these enzymes. _ .X - f‘ X / . T! r! x f \ J/_ H ‘ ‘I u .. \‘I __ .1 “I! )aJ/~ r i /., I \ >‘ f;- r r{- .1 hi, \ ' .III 7'1"- I”. J- .P‘FT—J \ /} .‘Jf‘ Hi i if"! '2 x __-:f . _ , a . . - ._ ': l i' 7 "’ ”(I-fr ”a! , ' I’ \ L -\ " I CT-Er ' ? , 'C/J'r‘tr H a ”ff 1 a _2 :3 |——v--' II. "r/ (— J L) ‘I f/ t I {X .'-{? Y! r \ E: l I ' . | 1":- Jk-I-J-‘J. ‘Ii 2"] f‘ E 23(6) Briefly indicate what changes occur during posttranslational processing of tRNA and mRN A. f _"‘. ‘J / x 3" r ! j x i “ r“ r 1727: — 1 c I "a _ ' 1 f f ' f ’ n I I L .' I/' . L.. n) I (I ‘3‘: / . - v; r r n .1 x 1"- £ f! If“ I’. “I X. f I X f, / f _f._ {b I 7 f, (l - \ - v 1 _r h, _‘ a! .i , 1 ‘ / f‘) 4. 4 F I { o 1.. t J _ v a * ' ‘-/ 24(8) Indicate the reactions which form Okazaki fi‘agments during the synthesis of the [aging strand of DNA. How are these Okazaki fi'agments further processed to complete strands containing only deoxyribonucleotides? What is the role of DNA polymerase I in this process? ': I" A/J/llj’ll 14,-? .3]. I I _ I," (Xi/.- II’ 7/ 0/\/"I/",-}/ .' . j .' --, ,3,! /' C 7 I 1/ j; ,4». [in 911.3,. (,3 33-132,. [3,3,313/ W... 2 ,; 3,1,3}? ( 1W: 5:? 7: f: ,_,,__ 7 . ~— i. 3 ,3 ,3 ,3,» ,3,. ,- /.__. .1, 0mm» DAM 9' 7, £9, 1‘- 3" J I," 3,. 3'" _ 2' _ . _ -'l , _, f7 09/»; l flA.-’Z«—, y, ofa” _ /.Ar',*7/--— / 19/1/94» LAW l x /" :9 _-’4 'L/- ‘ / ’ 9', - - w '-' 1- - I, ' A“ ”(3‘ -” f; we: a: / (/ J'Zflo’ J’/§---’:” fix 41/3? - , ,4, /r 43'" 25.02) Make the best matches: fl/ -'-’ 2-" .2 .34» ("fl 2? AVE/"’1 {,1}, 1/ z} .- a. EF-G h ATP synthesis b proton (pH) gradient 'E’LN2 reduction 0. EF-Ts NOz' reduction (1. 238 rRNA Leptidyl tmnsferase e. FeMoCo L displace bound GDP f. chlorophyll g heme 26.0.2) What are the five stages of protein synthesis? Which takes the longest? Kati—flag; 3‘ 9 M72; 21(6) How does the protein synthesizing system reduce errors in the sequences of proteins produced to an acceptable level? At what stages does “proofreading” occur? Explain the process(es) involved. l. A(_'-l:.,l«£l'r3%"- (oat. [-85 {RNA ”all (tofJ’f/Cf 4W! I m) “C'lch-ft.’l12'-l'tw.f’ - _ 9' golfer?) for bailt hubs—t £62 ZjZ AJc/Z-I‘fmmf {J whim,- Brig adjacent ”(to flcj';VrE-’_ fife, fYOolmfi-E [tjiolrbbggj “j ammo mini ’15; 5Mall€t‘ l":OY‘/10[Ojlrlf?“ _ 2 - Elucir’lj 3? :Fl‘It-flpr'mn’yélmioo ado} QI'MZJQX '1}; pH; (prion it? A 571% {molt-‘65 Jg/szfi) ofafew lung-”win. ,5 we“ *0 calls“? w‘mm W73 To clggmgm E‘jl-omfwfiaoly; loom} f—ofmrfliél’g Jelly? Meow-e, 617]” P CUCJWEJZW? a A”; ssoczafl s'o-w. ff EF-Tw 60¢). 28(4) Ammonia is incorporated into metabolism by which enzyme (limiting nitrogen)? 29(4) What compound(s) is (are) the source(s) of the two nitrogens in urea? 30(2) What compound is the source of the carbon in urea? #60 ._ (/60;w 31.(2) What is the chief function of the membrane in chloroplasts and mitochondria, as opposed to its function(s) 111 other cellular structures? Mwa 27:42 /€/} 4f fifljZ/«K’Q/g/rj ...
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