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examk - Fall'11 CH370 ICH387D Name[1/51" X Hackert Exam...

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Unformatted text preview: Fall '11 CH370 ICH387D Name [1/51" X Hackert Exam H UTeID R = 8.314 x 107 g-cn12/(sec2—mol-K); RCF = (1.119 11 10'5)(1'pm)2(r); s = 1111.1121- pwaicr = 1.00 g/cm3; s = M(1 — v’p)lN’f; (Ilcr)(dcrldr) = Mm2r(1 - v’p)lRT; A = AIJ exp(-kt); k = 1.38 1110'23 J/K; 11 = 6.63 1110':M J-sec; KC/Rg = 1l(M*P(9)) + 2 A2C Ac = (AJ 11 1.)/(a 11' K) ; n = 0.01 gl(cm-scc) ; N0 = 6.02 x 1023 (Note: Set up equations and Show work to get full or partial credit on all calculations.) 1. Fill in the Blanks l TIF, circle your choice (2) Identify the four color results that one can expect from a typical DNA microarray application to co111pale“nor111al” cells vs. “diseased” cells where a g1 een dye marker is used for the “normal” l/ 9111‘“ cell sample and a red- -dye marker‘ for the “diseased” samples. '11... A) 41— B) _fl¥_ C) Ir” 2 D) {11.11% that (1)613 F Automated DNA sequencers rely on a fluorescently labeled dideoxynucleotides to identify the frag111ents. 0 1’1! A (l) TF Most commercial DNA mic1oa1'1ays employ short sequences of bound 0— “RNA“ "“ ”unwind (l) T CD spect1 oscopy for dete1mining secondary structtue of proteins nounally employs wavelengths f10111 190 to 2401111111 mm. 2. Radioactivity: You have a rare, very unstable isotope of sodium (sodium-20; atomic number 11). After 30 min, you 'VB\ find that the radioactivity of the sample has decreased 90%. 0 \1111-121 . tZS‘Q, a0 f” f .11- A) What type of decay would “you pledici for sodium 20? E “3’31; 111 1’\ t 1% No i “7N8. ‘l’ \5 (4) What would the daughtel decay product be for this type of decay? Ne, (“20 X B) What is the decay constant of the sample? 1. (.3 O _ 0 . . . ‘ 11.- 14.)“ ‘1’. 19111-1 ’52” 1. p (4) Show WOIkhele- A A Q, bills k to '1: [GD 1",.- 3 gm N10 ~~~ \R (15011-1111) / 0 711 (l 911“, 11 (1” 1).) 01.111 11.1,. 1.1.... l l C) What is the half—life of sodium-20'? (4) Show work here: LA 4 f (9 ('1 r") h» [Ch “a, 1M "43-" ngole“ \ M 9| 0 WU A .1) . (Q 11113131130 \ Ol<\ 3. LSC: When measuring beta emission using LSC (liquid scintillation counting), it can be said that you start and end the counting process with electrons. Briefly describe the sequence of steps that take place to measure the betas using LSC. .. 1‘1: :1"; 1 | 1.1. (5) ‘5 11.1.1.1,“ is; 11'. 101101 3 it 11.11%} EZKQ (We; 11.11.11.111. l; m 11-1 ftlt 1.1. lb\\ 0\ t) 1.151, {31 1i-.. .1 1lrr1\‘rtrr1\ l 9‘ rill] l [1.11.01- 31 lilo .ola 0.16“ka { l, (1 ,1 (‘1 (1%" {I {Q\ Q”- l i" (Yam \) PWW—ywfiwmflmww 11111 1 llitfllt'1'1wr All‘t‘fl m (Q) (\(lelcilm) 4. SDS-PAGE A) SDS PAGE utilizes glycine buffers. Briefly explain the conditions and rationale for using this buffer system in both the “stacking” and “running” gels. 4 , ' __ _. . , ( ) "%\10\-le.1\& t-\ 03* (. Q“ A" (018))“ C?\\)1\1Al 1’s hf tl\1 ml 1...? if); c{ \1. l Qt" (it? t A 3 “PRO 0 (1 ’Ac- 1-1.1 (11 t 1"l30111’ntl‘ l RINK/‘A‘ifl-S (8K Q R“ A" q\ Q)K\/U1'\rx.( ti; tifif‘xtxl ' lf\6'1111‘1..', 5.1;A1,\3. Lg, we) C‘- 6’1f\_%\_\,‘\ Q‘ Ufa/X JIM B) Which of the following is a commonly used “reducing agent” used for SDS— PAGE. C Ti) A) Coomassie blue B) N,N’~111ethyle11e-bis-acrylamide C) Sodium dodecyi sulfate (2) @JDitl 1iothreito] E) Bromophenol blue D‘“\ T C) in SDS- PAGE, compared to the stacking gel, the running gel 15 usually. ( )\ @Higher pH, highei % ac1ylamide B) Lower p11, lower % aerylamide (2) C) Higliei pH, lower % acrylamide D) Lower pH, higher % acrylamide D) What can you conclude about the subunit composition of a protein you havejust isolated given the following experimental results: SDS PAGE shows two bands running at 23 kDa (01 band) and 50 kDa ((3 band), with both bands integrating to nearly identical stain dens my A gel “filt1ati011” chromatography 1esult gives a value ofjust over 200 REWWE“ 1)};le ” ‘ 33? (Sit/tit“ '1”) MAG? ‘1 f) (ll-Ml . 3 Subunit com osition e. 012 2 95 1' E) w; . 1.1.} a () ’pi‘i}; ( g MB%)(.\\ ' Emmqu SQQA/fi) {)‘f/‘x “(13th 5. 2D IEF- SDS PAGE. j You pe1fo1111eda 3D lEF-SDS PAGE experiment on peptides P1, P2, P3 and P4 with subunit / inonfpimic masses of 65 kDa, 30kDa,135 kDa, and 90 kDa Note: it 1s known from other w01k that P2 fo1 ms din1e1s and P4 fonns tetrameis), with pl’ s of8, 10, 6 and 4, respectively. 011 the figure below sketch the expected outcome of this experiment by drawing and labeling circles to represent the predicted results (locations) for the four peptides 011 this gel. pH 4 pH 10 (1 EF) s. r 11,1: LI to Ex" 1 O 6. Piots: Conside1p1oteins A, B, andC that exlnblt the mobility behavim shown at light, which p10tein(s) log U A can you conclude carries the most total charge under the conditions of these mobility experiments? (3) l); E lama . amok ‘c‘a1}\4‘>i\\ I; mobilitv '34, gel ‘J\\§\«'\-') 3 7. Units: Conside1 a propeily folded, 80 kDa globulai protein. Estimate the value (within one 01 (161 of magnitude) and give the units for each of the following par'ameteis expected f01 this protein. (4) '31 .W -27 , A) D~ iQWHWB) f~ tt) gate. B) s~ «3333 D) radius~ '3in fl 41 M3 1 8. Analytical Ultracentrifugation: A) The three optic systems commonly employed in uitracentrifugati011 experiments are listed below. What property does each optic system measure? (6) . . Schlieren optics d 333/313“? 132 ?\ 33 ’3 3" ‘3 3\ Interference optics I; 0. Absorption optics it... B) Sedimentation velocity: Estimate the sedimentation coefficient (3) of bovine serum albumin if it is found to move from position 1] — 6. 78 cm to 1'1—12 — 7. 77 cm over a time inteival of 165 11111111 at a rot01 speed of 155 000 111111: .. rammwmw- (Assume. Pprotein“ ~ 1.32 g/c1113;p301v— 1.00 gfc1113; Vbar = 0.72 c1113/g; T: 20°C) 5.1 11111112.: imtn 2111111113,, .. 1 (1'; (7) 3’33 M“ “mew 13531105: 1052111. Q‘tt’p. . 111111 11w? ‘11'111111g3 :1) ‘1 3&1... m (3; 9.2.13)?“ 111:3 £11113 :1 1111 11111111113. (:1; 1,... 211111 E) 1111 (1 W.W.agraa w... 211 33 t” m 1.2.1 31 at? .-..-5‘; ’11.0.\ (310113}- ...W ammo: Mair/1N“ (2) Name the two primary factors that influence the value of “s”? __,‘§,1 -.. { 11-1) 5.31129. 3‘1}. fig) 11;) 1 3K {to 1\ 3K 1'; .2 (1313?“ “715034.13 .t§> 3’ (3) [333 tit/16331 C) D and f: Given the following data and R111i11 IS 35 A for this protein, fill 111 the boxes with l‘, ) K'JJ {mpg-id. aux: 'wwtsaa fmin, and the fi ictional coefficient latio for this protein Assume T—1200C, 11: 0. 01 gf(cn1- -sec). Sustance Moi. Wt. v— barcmslg) D cmzls t‘ (g/s)l‘1nin fffmin 1Ratio Unknown 68 kDa 0. 73 0.125110 6 :3 2121.11) 0.1.1.115"? { (11.1 ”-2. (8) . f. T" (3)313 ta 111111....$11111. ‘” - ~33 53.11111 11:) 35:1 " (\ “if 13.331333333363511, 03% 11 1 1113.194” 391113) 1.0.1233 1 2»~2..M... 2 .1... DC 1101 22:.» :3 es 3-“..- 3-. 112.352 6.1; .1 t 1 .1 9. CD: What kind(s) of useful infonnation can be obtained from a CD specti um? (43 (1.1“. M. .. 21112: 31:12:) it 1111,, .. {)7 33319333333" 1 E E; 3'\ V \'3 f} V\ it“. J§\3:\( k\ 3513331: t1\' ““11" (311 gig. (13313-3 3133 11 “’3‘"? 33333333333111 \. 213122 <1... (<2. M3. / 1:. 21'1“\\ 1.1.x) .13 M. ‘Iiil.§.\)) 311111111 1\G\\3i11‘11 1W3 HQ\_K\1V\;1 {<3 flax ‘i (1333} 9 \ '1 “1.11 \ H9 10. In a sedimentation equilib1'1u111 expe1i1nent, a ptotein is cent1ifuged at 6400 1])111.The teinperattne of the system is maintained constant J20 oC and the density of the coiloid IS 1. 24 thv kg/L, the density of the diiute soivent35100 g/mL, and it is known that 0.500 g of sediment displaces 0. 361 mL of soivent. Using 1nte1fe1ence optics we determine that the concentration at 11 (6. 78 cm) to be 0.15 mg/_mL and the concentration at r; — 7_. 45 cm to be 1.32 111g/111L. Calculate the 11,1",me .‘fi ”WWI. .. WIN-(HEM moieculai weight of this p1 otetn Place answel 1112112ng ‘1, m :51) w. "i ,show kbl “’0' cow 11.) (111111312111 .. (291(70me [33311.11 fifi awfiose ' ...m WK,- mm (00.5.9.1;fl WV (8) T” 202. 21211 11 1113,51 sow} ”11:22 1,1; 11111.1 $3,0'3laibmkorzla S’M £1)va " 1' 1.1213 UN) 0. ”3me :3 a) __ ”mg—WM W-W- ,JMWW n._.._-m..‘....~1.1m»w WMM.J.,.,.1,.w_-Ac.~umm W421 I. W... WV W W MK. ,- W1MWMWWMWM- (“3‘1 51R”? «W W-flmmww‘w‘ ”M ”Ma-.Mrawzdy A- mWw/mwwM-wwwnra" mm.- 1&- 1.1111131111121111“) mg 1 (fl FNMA “5 0110qu Wheel 11. Concentration by Interterence Optics : Consider a centrifuge double sector celi with protein soiution 011 the sampie side and dilute buffer 011 the reference side that has a hairline crack between the two sectors so that the buffer can layer over the protein solution once the centrifuge is turned on. For this experiment, the T = 20°C, the rotor speed (1) == 4500 rpm, the radius to the sample optics section is 7.30 cm, the cell path length to be 12.00 mm, A = 546 nm, and (dnfdc = 0.186 (go/C1113)—1 . Using interference optics to monitor the 11111, the results shown below are obtained where a = 12.11 cm, 1) = 14.95 cm, c=17.74 0111, d : 20.58 cm, e : 23.44 cm and 11 = 1.9 cm. 94mi%%\ "MW V3310?“ 2 ) m ‘ Manhotmn 10mm 2W3“) a) Calculate the concentlation of the protein sample at the a110w( 1 ) 111 mg/mLfi 0111 the data given above. Piace answe1 he1e [I 551 111: 5 Z {1% 3,5110“! win ' l -WNWWW WC?) 11‘3 2» 3.1. (y, :12 0‘» K (EPIC 1110(6) 131.1 ....E 111111 1* New 1 “341,2“151‘1 11111,?»bwma 1.11.1, M, mm (.11 than @1111 <2 Q3213 12. Light Scattering: a) What is the relationship between the intensity of scattered light as a function of the wavelength (7:) and distance from source (r) ( I is proportional to 9:, or ilk, etc., similarly with “1”): I» l (2) i) Wavelength: I is proportional to i/ 2] l ; ii) Distance: 1 is proportional to I}? a“ b) Identify the kinds of information that can be obtained from “static” light scattering vs. that from “dynamic” light scattering experiments (2-3 sentence limit each). i) Static- MQ/CL3M»£§ alasawitlt Magwlm a.:a;<3\fi with Maui. in»: (33 -N\ WE law yt’t’ill'tlw (low i50nm\ was}: stat, a5: ‘i‘cth twin 6% $tm¢vtfrm {xii 5;) hitfmtx. “MN-8A0“ QiJQQJMAJM-LQ- 6X Lff: “Await ii) Dynamic - than” (3) (so 9 M twat»? “saliva ta»: 3“»: 5: Williams am: 3::3: all as. m 6:: “we, ditwwa: W»: “ a “ :::::,, KR ‘1‘?“ng : l1" .. : Yujhig' Rh“ £71 (ii-Q Emit “AA VOA: WNWKV) a N1: (fa-:3 i (kg-t ws ‘5‘ 3 V‘ 0) Why are both light scattering (LS) and refractive index increment (RI) measurements required to measure anfif‘absolute” molecular weight using LS methods? (3) _: (in Q: ' : o3 LSWQ»M»K»CM i é (Tic) " 387?} 5g“ “3" M a C—Mfit m R317? : g »: K (gig g; “(a)“: 1?: “if? d) Why is light scattering a particularly good method for checking for high moIeculaigdontaminants in 501mm}. $.illllP..i§§Zm. \. . » |\ a ‘l ("5) ”it? Etta-Via a: “with-ii at): MA; x): a. mix-«M, 653:3: Rig : (3) (Please Sign yum mum on the back near the top oftht's exam in a manner that you can recognize for returning it to you) ...
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