bmb3100-20010802-THU - BlOi‘BCMB 3100 Final Examination...

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Unformatted text preview: BlOi‘BCMB 3100 Final Examination Thursday, August 2, 2001 ‘|.{2] Name two features that distinguish procaryotic and eucaryotic cells. ét'ft'c‘fr‘a‘cfllr‘; (e? are” much {Mm rio'ffc cue/73 tic-“0’6 it 51?” -”-’~'3(”r9"‘5 n :‘ don-tall? orfifi’ltfiflfs) ( 4 n n a, cgrfisér/Fffih) 2.(2) What gives water its unique characteristics as a chemical? r I'll-'5 ['Lfi'xfién bowl»? CRIN-{5:17 -’ Vt. Perfrfld'iflf’ta U" 570 2L0 firm/1E} 0J5 4&J43J6’z 5- 3.(8l The following mixture of substances was subjected to gel filtration and to SDS-gel electrophoresis: substance subunits x molecular weight 1. hemoglobin 4 x 15,000 2. bovine serum albumin 1 x 67,000 3. alcohol dehydrogenase 4 x 35,000 Which comes out first and which last (1,2, or 3): a. gel filtration: first 3 ; last l b. SDS-gel electrophoresis: first I ; last 2g 4.0” Draw the structure of the peptide LRY at pH 7. Circle the peptide bonds. 4.. ’14 “if "" %N_6 ? C “.030 f 1' CH1 CH2 " CH1 4- H é: will a f . NH 5.{4} Your text names two factors that account for the Mtg of the rate acceleration provided by enzymes. What are they? flax w: if“ 12%,; (7f- t/ J ' /- v. I z: £ 'Z;:1. V1 ’fifl’ft-‘Si POI/L .3 t 612) Consider the chymotrypsin mechanism. What active site feature differentiates between he various serine proteases? The J’SfrfitT-&FCP‘\‘] {C’OCRQTH if) deF'E’Y-Bi’tf, 7.{5] Write the structure of NAD“: 8J2} What does NAD stand for? / 0/) . “_ 2 L ViiC'ththJdm:d[€ den/finfl’ie “NAG ('0 2 5M4) Given the reaction, Ubiquinone [0) + NADH + H" w Ubiquinol (0H2) + NAD”. Calculate AE". £0! Q‘thra‘rZe’ —e em, (9.04 [it/140+ + Zfllfi—Z e, we» UA‘DH-e H7; #032,] ‘ rettsx‘st’. ; ’ ,t 031 arm: £15,“; + 0.3! u”. Tabla 11-4 Standard reduction potentials for some important biological half-roam‘ons Reduction half-reaction E“ (V) Amy! CaA 4- CO, v 1-153 1- 2:9 -—-a Pym“: + CM -0.‘8 Fmdomm'spmach). Fe® + a3 ——a F¢® -D.‘3 2116 . 2.9 -—~. H, -o.42 a-Knoglumate + co, + 2&6 + 2:8 ——- Imam -o.Js Lipoyldchydmgenm{FAD) + 2H0 + 2.9 -—+ Lipoyldehydmgenm (many -o.J4 RM + 2H0 + 2:9 ——u NADPH + H6 4m “06> ‘- 21-:9 + 2:9 -—a NADH + HQ -o.32 mum ~ 2H6 + 2.6 -—+ Dihydrolipoicacid -o.29 Ghumioncfoxidiwd) + 2H6 + 1:9 -—+ IOluuLhiomU-oduced) ~03: FAD+2H®+2¢9-—. man, -o.22 Mva’ure—am, 4m mahyde+za®+2c9 ——» Emma ~on wmq-zneuce —-r Lacute 4m Ouiooc:u:c+2H@¢-2ee -—9 Maine 4111 cum b,(microsomal).F¢®+ :9 --a H9 om mnH‘Bnfi—amm 1103 memazuenfi '--) Ql'l, am mummhoruwne9+ :9 ——» 3.63 ' om Wcl,fie+te—b F00 032 Cylnchmuur.Fc®+ (9 -—9 Pea 0.23 -W5.Fc®+ (9 -—b Ft6 039 QuhmufiF¢®+a9 -—-D Foe 0.36 mPc-zuence -—I~NO,9+H,O a4: Maseru P700 0.43 ['94- c9 --h Foe 0-77 no” 2110+ 1.6 ——.— 3,0 on a 10(2) 00 reactants or products predominate in the case of the reaction written above? '. 'FJC 0.6:): '5 s“r"j”—fst'f€] ~ 11.{4) Draw the Haworth structures of two different ring forms of D—fruotofuranose and D-galactopyranose. H H052? O 9430 HOfL‘C 0H , 0” oH‘K @ 5 D“f“’“"t°9(""“m OH CHXOH 0H C/HQOH Ckia'gOH ' O . OH 6'0 in so Ho/Dd “0 0H 9 WWW 0 OH OH \ OH 12.!6) Write the reactions in glycoiysis resulting in ATP synthesis. Name the enzymes. 13(6) Write the reaction and name of the different coenzymes invoived in the oxidative decarboxylation of pyruvate or alpha—ketoglutarate. 723% r 622 Mpg» _ P log/42:5 7L gflO‘S/L/v" AMJL > flaw/fffi @A’ + @+M40H+H 7% @l’fl’fc flafl 14.16) Write the reactions i?! the three enzymes which convert NAD+ to NADH + H+ in the tricarboxylic acid cycle. How are the intermediates in this cycle formed from carbohydrate {pyruvate} and amino acids? Wee/22, + A/flflfire OZMW %/i//4W/+/4+' 7» + . or’--/</£/oiMWg/ 7"IV/‘70 ——=2 wax/M + die/f Eacam/FSQ/f 7 15(8) Briefly describe the pentose phosphate pathway and indicate three functions of this pathway. Gjawse é P % N/fflfl —9/\/%w/3fl HJ g jZ/ngfi/ aflwjflwflfflyfi 7P MAW/l; Name A”? 4522/ + (5255, 5/0 flak/5.6 579% Jig/(wax, 5 P 5-77 éflyWfl/éfl 3/” %~ £JWZ’a/aje 7/9 gflgCg/{MWJflL 577mg 999% X i9! 5/94; FMJJX5K+ @Mfl/ggéflofi.3/J SWMM M949; Maw ' W Wm; fl / W 29 MW fl Maw 16.!5) Describe the pathway of oxidation of NADH by oxygen in mitochondria. mm a Fix/wow gas» F66 . 7 2M 17.18} Write the reactions involved in the synthesis of triacylglycerol and a phospholipéd. 0 5&0” g 925205;? Wee + Mcswaméiq * ma 45% . f O . r? " 0 939m}? 0 6/4200? .0 1! 4 n H I @094 7‘ Rosam' «*9 #953,“ _ GHQ-20H - Chadd/z O 44 09PM M100}? /7 (“ppm w> + #603? éflz‘j Iii—Ov- g a wad 18.(10} Write the reactions involved in the conversion of butyryl S CoA to twist! moles of acetyl 8 00A during fatty acid oxidation. p , 2? CH3 6/12 GHng Egg/4 +540 ——> CH} 6/7": O'HCSQflv‘fZ’J/fl @ C/JZC/H ' W ’9 d 3 07/ iféfifl + #20 —-> (W; eye/{10569.4 CW3 6,4524 55% 74 A/ 0”” Q ’9 O 25 /4 fl H9 626/} C‘- WZC I: // ' 0 6/1/34 Off; (256/4 vi @2454 aa/géfygw wage/4 19.i10} Write the reactions and describe the role of citrate synthetase and citrate lyase in fatty acid synthesis. “ii/“CW5qu dim/a 7L myflwwk f“??? :__ 20.(10) Write the reactions involved in the conversion of acetyl-S-CoA to malonyl— S-ACP and then to butyrvI-S-ACP during fatty acid synthesis. ,4xX SéflfagryWWgahmd$763&fl¢flmwda Zg jéfl 7L. flcPE—y fflofl+ MASH 569/4 71. flap -—-=2/224W5r4010% 7% {mafia/4+ WWI/40% «9 64; eflc/fl/ 7‘ ' ¢ 9 p I 9 - d@cu%563400 41% széS/icmwpfl/s 9’” g . 9/; p UGO/‘2’ (if/Le 5M 2? - 34/7’HW45W7L 6/ 0 6H @H- *0 8 J9 *Qé/GW-f Map/7f —-) N/m‘; M ,0 21 .(12) Given the "Z scheme” of photosynthesis: +5 xb 31 P072 31f)?! / ml; {7/ 2:40: . 6 V ‘03 KO m I K4 mr 5 2: 0,34? Identify the substances with numbers: 1 Mr: “'60 m/P/rf'x 2 P680 OXIoJOn 3 [Q [I 8325] 71 4 a: c: -}YOV‘/1»2- Effowf/QX 5 (“.Lq'nin 6 7 O 1' itffd‘nf 2248] Four integral membrane protein complexes are involved in producing 02, ATP and NADPH. What are they? grew I (of COMIC/€95 SySfEi/V! fl- ,0 n+0 C {C(j‘. J a f) (7 (5+0 £77? 9- £5 (7, SJ“ no true, 23.!2) Write the first enzymatic reaction used by C4 and CAM plants to reduce photorespiration. / (:0 ‘f- (tQS/T/°otimji(f,J4V'&Mf-fifl ~9Ljitf’ll06‘f'5’e. ; (or; #633”) 24.{8) Describe the sequence of reactions catalyzed by DNA polymerase 1 and DNA ligase which convert Okazaki hybrid fragments to a complete strand containing only DNA. 0M47(flma0/w4)fi—e 0AM;— (w— axy/9,7 % WK; 5M6 cm/j/ZM/D I (3/7779 - DA/flr (em/,4)” we”, ——9 p/i/Af ( DNA-5M4)” + M“ a 7'77" 3 0779 I - I ’ 3 . DAM r (DIV/4 flN/i’fow 5,0 DNA) +A//Z§;_—¢ [QM/17. (DA/fl “any: a” + £33? A/M F 25(6) Describe the reactions and enzymes which synthesize Okazaki fragments during replication on the lagging strand. AW {DA/,4)? + 67F ,_>,. 0AM gel/4”) + pp; 077° 7 (:77? am? A {DNé/VN'QW + 95720 ——-> DA/fl7(/9M4“DM/4)77 + W; d U? @6779 Ma, Mflm/ZM [QM/4 . 1 04/4 M 14/— M‘% 514%sz 06 W, / Xxx‘w' 26(8) Briefly diagram the replication fork and indicate which DNA strand is synthesized continuously and discontinuously. Be sure to indicate the 3‘ and 5’ ends of daughter strands and the proteins or enzymes involved in forming and stabilizing this structure. I . _ _ 56,17 414,-”. £3 {flaw/1:6 ([fl'z/ZKW 51445 J J ("*‘W‘ ;/ 2716) Briefly indicate what changes occur during processing of rRNA, tRNA and mRNA as they go from the nucleus to the cytosoi. HAW/4 ,éflA/fl Wfl/l/fl I) flmzw 0 - fjgwmc‘f c).de Mac _ £1; 5 my 39m a2.) % W 7WMW‘ 3% We; 64:.) I ' WW 3’ 28.{6} Name and describe the functions of the three types of RNA synthesized by DNA dependent RNA polymerases in eukaryotes. M We WMMfl, we a ‘ -' ,4 Mad. '?-';2’4 fl: M W06. W/Mi/(J 29.(10} Give the unction of the following substances involved in protein synthesis: a. .‘ R’ej amamfé’, J;iP(aC@ 5?. {F'T5_. I dug b. lF-2 , _ ' { {flow/fax)“: .. [Vex é: q/r ._ _. Jam; has? 1 ‘ fl/ *1, 6,79 Com IV} a ‘ f m- 5’ #1; :05" swears-£- ML 7546 pfirjzg 2:444 é j Qq III/39%ya/7n ‘Me ma’fiSflW‘flV‘ Ext/f? 0*? {[75 J P" “950mg” c. [5:72:53 6:777 canaqokx Shut/1‘5 Lf/tefwf’lzfi/y/ffifl/fifrém ‘5ch1 {0 "Me ?51'{£55/Ufifim f/ze. xaqessemjafflf/fi 63» 0mg). Cu—-..J L . CEF’Q “62779 [3;sz {o .e 2’3 Sift.) d. agitgzg {‘0 {Le 44 521’? when 1"er Coo/m4 7:; off 243 IQ 979%,) Cam'snj ljjrofiesis of #9. c1.” 5 EF—m éj oils/0420:?» GOP so m-Mwow A‘IEV‘HS +119, JMCISSEVI J 8. Shine-Dal arno sequence I A g fey“ EMA so 12/163, 51me 59%»; :5 4,12 the ROS/"1.18,. 30(5) Explain how the protein synthesis system ensures that only the correct amino acyl tRNA binds to the A site in the ribosome. my. {:20 —flpzmmsm» Hit/144 ‘9*""/‘"{°X 5" flfli A jig-[1,2 _ QT? {yam/:13}: OFCdc‘i/S 54;;qu Efficaé/‘mv rat'CJfi’C’C-‘f fl' :cm'no an] 05:7? 5*? 0V5» ébficc/fcbr’hmfédi? . 77 /5c¥5fi-flf‘0 M (Fr-7:2} (Oriya/va r“"5 4/50 50“) 79.qu , - w Ir 3? _ r; (a 24/3,} Sc'rvnfl/ amt/(rat'fo OCCd'Nfl “tiara/70f? a éomj/fcyrfiofo} “I 1 HM” A36 iv 9 174-2, 5/ z‘fce f1”? 1 51». 6334524147 don/at. 54/5“ W354 r ’ J 7 I fl figfif:O%93/} éan/Ca/n . Co, f I t ' a 31. a)(4l Describe the reaction catalyzed by peptidyl transferase in terms of its mechanism. Ari aUZP/mimg in '00 {:ch liramsjzevqsg rewroqu I (c Fr’bfbfl 3(0)“ fltéfémimo my. 031 (“is ammo (Lch dfiacheg/ ‘f’o fir; 'f'PJIM [90iwa 'éo [Sfer 7n fl,er rtr‘bospdmg} . g) ammo orort Inf—o ca. nag anfzj)./€ w [322,4 {ngSff‘m/‘r U af’ffléj'fi'h . (arém: / of flap. ammo aciol a, (25.5185/14-0 {Zia 5/ {fig/,4 I Mlle Part a 77.6, (95:71.9 ammo adc/ Es 757VW’35][«“7‘”32 f0 (amino aci'd’ In fi'ég, A Strife) maéfvj cab/beycffdé 60:? bH2) What is unusual about peptidyl transferase? It Is as riéozjmg. (235’ rFEN'A) 3242) Approximately how many moles of ATP {or equivalent) are consumed per amino acid incorporated into a protein? 4 33.(4) Describe the function of the ATP that is consumed when nitrogen is reduced to ammonium ion. _ m, AT? é‘;v‘:(‘25 1L ivrfrJ—‘E'WOSF facififejflflw J-IAJJ'T-sé‘rw'f' r ‘ .u waffle (“ff KL)“;ng if; r2342: c'371g9i-77L‘b. 5:0 :21 (13m rake, / LjJ.?FTd/_fi0 1’? £3}??er ér.“ {vino/'51». raga-ftp] c—‘f "(f/r! Z/Fflt’l ‘ ' A 34.!4) What is the reaction in which ammonium ion is incorporated into an organic molecule at low ammonium ion concentrations? Name the enzyme. Agni/4+ +I5’Af7izi’y’fl7tg '1‘," —--*'—-"7 + 4-3 [{{fknox’d’lfi J _ lcfffll’ifi‘zli’.‘ {- II C 5) Sgt/[M (2405f, J 35(2) Give the reaction in the urea cycle in which urea is one of the actual products. fig)“, “.162, + MILO __._.;~ (firmi‘féimé ~+ {ff/Z261, ...
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This note was uploaded on 01/31/2009 for the course BIO 4200 taught by Professor Dr.blake during the Spring '09 term at Gwinnett Technical College.

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bmb3100-20010802-THU - BlOi‘BCMB 3100 Final Examination...

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