4033exIwhitekeysum11

4033exIwhitekeysum11 - BCH 4033 Summer 2011 Q 13me i 6:59...

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Unformatted text preview: BCH 4033 Summer 2011 Q 13me i 6:59 c9 , W" M” Draw Thr and Pro in their unionized? ates. React the amino acids and draw the dipeptide Thr-Pro. Use é “ curved arrows to demonstrate electron pair movement that leads to the product. 3 i at I t H Mifiw c «a via}er cw aerate» It," I Lk¢j revere o a \ 2 M; N?“ J til) 557;: /«~’% 2. Label the oxidant (ox) and the reductant (red) in the following reactions: f’? V ,. é; ':flE,.,/ a. cysS-Scys + DTTHZ ——> 2cysSH + DTT , em MW OX (fit V’ffkévté’fi 6' 3‘1, Vi 5’2: x b. FADHZ + CH2=CH2 —> CHg—CH3 + FAD ) wx’VQ 0 2g “YA? GAO A.“ ff” #3} Complete the following purification table for a new enzyme found in the kidney. The tissue is homogenized in a blender with buffer and a crude extract results. Show a sample calculation for specific WM activity, % yield and fold purification (purification factor) with the result of the calculation. 1000 were} 300 117,000 a a get La 6 Ming 5 ficam ,( I l l ‘1 3 Q—@ 5 in g “i “2 m <55 jWét‘ ix”; “33“ ii A g; E 2% fr 9' My; fix fl} r "k t r fl What kinds of forces would occur between R-groups at pH 3.9 in the following dipeptides (other than London dispersion forces). Indicate the overall charge on the dipeptide. ii. leu-met g; cg iii. glu—asp db 55am; ) Given a mixture of two proteins, A is myoglobin and B is hemoglobin at pH 7.0. What would be an 6%? easy way to purify them at pH 7.0? Explain and be specific. if, a 65 «g; itfiwifi” (fetid “WM ‘41“? r ., ryfiWwW-UZM’ ‘mgwyw " if Force type Charge ; i. aIg-gln t , , A Q? é‘mmflsrfifi'w fa?“ wagging Lye 5‘? Wm 54mg; {Vi Kaila? /§@W,J a am if ga a; was firm fl. p15, ,5: 0,. g} ‘6 A) f 65;: gaggxfl 94%;; fig l W mg jvffimflx y A; ,r-Ma If,” ‘ z‘, fmflwf 53>“? We BCH 4033, Exam 1, Summer 2011 Z 6. An unknown 20 amino acid peptide was isolated at pH 7.0 and when administered it has the ability t inwww. .MN / //// "Q gallow one to read people’s minds. Answer the following questions based on experiments aimed at R 3 fig?» elucidating the peptide’s structure. Be specific and include amino acid names where possible. R1-R2~R3-R4-Rs-R6-R7-Rs-R9-R10-R11'va2-R13-R14-R15-R16~R17-R18-R19-R20 Maw _ a. Cystine is found in the peptide. What is cystine? (Complete structure not needed.) a, 5% i ééif"_d§vg’w (A15 0%“ Qfiifiz; i‘gé‘tvxwggi dt'lwtlé'tgxz b. Trypsin treatment has no effect on the peptide. ’can you conclude? ! M0 l E>QW Fwdewt’iw 5°” «QM Wt; (up; (xv-scam?) l ' 0‘ f. _ . . u - c.,Sanger’s reagent flolEG‘Wed by ac‘i‘d'iliydrolysism labels a acidic amino a01d. What can you a‘cvigkr'iclude? , a, w a a . A. , L? e 2' , LS wet i‘luw {33 e w“ i I M “at “in ’3 i N “J “fre‘mthw d. Two equivalents of B-mercaptoethanol are needed to react with the peptide. What can you conclude? ( ail/«.5 Si? (—2 ..<’ I?!“vath (6?” /K£;4:Jw/Cffilr4u4 gamut?) blagéiisrta e. Draw the structure of B—mercaptoeth te its purpose? “In, H‘fi » r: [it-.1“ w e; j we é‘é/s‘t M, diet}; a e! @206“? {96‘ eggs” f. At least one [3 turn exists in the peptide. What amino acid is most likely to be found in this [3 turn? / (0W Mead“ Cf” é.mn g. Carboxypeptidase releases a basic amino acid. hat can you conclude? (:69 i 5“)“ M on? . ’ a,“ A“; . y)» . 7% Ar?“ . a». S at; L5 430"? a “e W rem-75: ; 4” W M I I: “a? u WWW! *6! h. A reagent is added to the peptide and after acid hydrolysis a‘ifluorescexnt gnino acid is detected. What is the complete chemical name of the reagent? Draw the reagent. "’ Y WM W...“ g“ «Z9, Dénicji 5.5.1 (:9 w 3' gig g r“ I I a an, W M g ‘ What could the fluorescent amino acid found in the part (h) be? Use the information in parts (a)_(i)_ fig QM (“Vi/read?“ til/ally éaMu-l) j. Draw the electron dot structure for CNBr and namé‘itf’Based on your knowledge of organic I, chemistry, show the first step of the reaction between the particular amino acid in a peptide that would 6 react with this reagent. (Use curved curved arrows to show the electron pair movement.) We ~ ‘ a é)» a.” (Let: i . V‘ ‘1 “W M 9 " a: a: ‘ f): k w? . t 9 ,- i: e: 62 a “if 5f“? a“? «3’ m Wm: eta? Me;ng ‘ ’ 9-» A, .7 r x I,” \‘x . . . fit A peptide is digested with trypsm yieldlng 4 fragments: Gly-Thr—Cys—Arg ; Val-Glu-Ile-Phe-Arg ; Glu-Phe—Lys ; Met-Asp-Tyr-Ala-Pro—Glu “T / Ta... ‘2‘ “t” (if The same peptide is digested with S. aureus V8 protease yielding 4 fragments: / g M Ile-Phe-Arg-Met—Asp ; Tyr-Ala—Pro-Glu ; Phe—Lys—Val-Glu ; Gly-Thr-Cys—Arg—Glu ‘4 (t '5‘ P, Pa P3 we fiwmfi: What is the sequence of the original peptide? (Explain your worm)...“ a. 15%th M W M C 4.2 We? ta. £55 at f g Ft ta WW mew. Gi‘; *7?er w flag a {vim} (Ema €9€ixuémqg «Mia‘s. \N I wwww,‘ , _A W "Minutemaw “we” \WMMWM... in a . T 3’ “$23: BCH 4033, Exam 1, Summer 2011 3 I, 83;».‘The following questions concern proteins with organized structure. Silk contains a large amount of what 2° structure? w A? In .T [’1 , gr 3' r ,t Maw-w! Lu b. What force stabilizes the 2° structure in myoglobin? H “’ he .t < é “” aid gait” “ gait @453 L: . . . . i s /","i c. The protein that hair 13 composed of is? fer: Vt I a x“ j , X d. What is the highest level of organized protein structure in myoglobin? 3 i (“a “1%? V”? j e. What protein exists as a triple helix? 5‘9 i i 5% a?” m f. Where in a Ramachandran plot would most of hair protein residues be found? Put X in quadrant. { g. What is the stabilizing force in hemoglobin that produces cooperativity towards 02 binding? 5“: if: We‘jger {we git}? her/,me y @eé’ww E; «h. What are the model names that attempt to explain protein folding? /% €\‘€V&w‘ci¢x tea, W1 5? “i”? “‘x it“??? at A? 'k. g i. Name a binding protein that assists in protein folding. t; axe. set are true at)- 2;? If 02 is bound by Hb and there is 1.5 mM free Hb and 4.5 oxygen bound Hb, then what is the fractional saturation? Show your work. M 4 l W, W ‘9‘ W“ 13,! :: x if: i“ n w M’aatwawMa-uw Wflm‘ifii‘<~x mg, L g t g: ,r M l r c“ (a Q tartar mite—w M 1 m x a? r LP \\ Hemoglobin leaves the lungs gfiiflng a molecule. What is the molecule and how is it carried? Be specific and use structures and names to demonstrate how the molecule is bound to hemoglobin. I V 5 a ff thnfifgéf, at, (3L (i 4 9? ts wt,th {mm 1’ , w la #9 5 all My i“ an H We eat PM in in ‘f‘t'wétim‘g‘efé » ~35" 1 y f1 * ‘M C! “’3; aw” WW?” Hi itjépkgfi ‘ M. WA 663%?" \ .5???“ liva 9‘ Qty” it“? ,, H \ ‘ fl: («1 MFR-w 5‘ fl BCH 4033, Exam 1, Summer 2011 LN 1M egg 10. Use the axes provided to sketch the titration curve for the tripeptide glu—his—phe for the range l-l4. Label the axes in the boxes provided. List the pks for the peptide. 14.0 12.0 10.0 4 - 2/}?1 1. Draw the structures of A" and HA at pH 11.20 for the dipeptide arg-tyr. Label your answers. " f ‘i , A 1d; 1. r’ r i” L? " ‘ 1‘37 Egg W a”) g ' F} g? by,“ X‘. A .0. am (gm - a w e w? 6;“ a 1 la“ 1' l a p, _ ,. a LEM} Ha)? ff tin/11 E 2 C: a: Mail Law) may v ~ g I 1 “ gm [H+l of HCl at pH 5.38? Show all work. ' C” A”? ’ "3‘. £3 “:1, 1? gig? 119% f 1.11% 1?”; maxing) a... A W, m; w “t/Al ' h 'd l 1 ‘7 L' 11 h h 'd “1” 3% 5% m ""9 f“ 23““ f 1Y1; Whatist epl ort epepti e ys-g y-arg—ser. ista t ep 5 ort epeptr e. 1 1, . /. 51-ij at. Show all work. [(9 "D m 3) “gm §M«%?aa_€a) c W“ ( A +‘ ‘3“ a I c? 0 Pi“ mm 2:: Ear; 1:: ram .2" M 14. Find the ratio of [A7]/[HA] for the tripeptide cys—ala—asp at pH 3.43. Show all work. Cr 5% 45 ’ 3c E: W Y; “9 ‘3 W} 4 f 2/3!” j v o .751 3 it? low?» a $3 w {3 g” m r , we» I ggfw~ V") 1% ,flAl 5. Draw the D— and L- forms of isoleucine using a method to depict the stereochemistry. gm" 3 Label your answers. ‘ @6413 U 1 11mmgwwar 1:; «« «ml? 1 *1 1 4“”WC ’19 Ht: t g “y \_ ...
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4033exIwhitekeysum11 - BCH 4033 Summer 2011 Q 13me i 6:59...

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