{[ promptMessage ]}

Bookmark it

{[ promptMessage ]}

BIS 102 MT2 Summer10

BIS 102 MT2 Summer10 - BIS 102 Name< Summer 2010 Last 3...

Info iconThis preview shows pages 1–3. Sign up to view the full content.

View Full Document Right Arrow Icon
Background image of page 1

Info iconThis preview has intentionally blurred sections. Sign up to view the full version.

View Full Document Right Arrow Icon
Background image of page 2
Background image of page 3
This is the end of the preview. Sign up to access the rest of the document.

Unformatted text preview: BIS 102 Name \< Summer, 2010 Last 3 First K. Hilt Second Midterm Score (100): Equations: pH = pKa + log {[b]/[a]} Amino acid pKa’s: a-carboxyl group (2.1), a—amino group (9.6) side chains: D (3.9) E (4.2) H (6.0) C (8.3) Y (10.1) K (10.5) R (12.5) Oligopeptide pK.’s: C-terminal carboxyl group (3.6), N-terminal amino group (7.4) ? v N H: 1. We hadthe following oligopeptide on our firstmidterm: P -N— W—H— I - C —T-K. (15 pts.) a) Draw the expected elution profile that would result if this peptide was broken down to amino acids using the procedure discussed in class, and the resulting compounds eluted, detected, and quantified using the column, buffers, instruments, and methods discussed in class. Label your x- and y- axes, label clearly each eluting solution. Label each peak correctly. Draw the peaks carefully, indicating their positions and size. “(2,547 Tun/‘4‘, 4*: or 'TTM +m§ (10 pts.) b) Explain briefly the chemistry that is occurring that causes the oligopeptide above to be broken down into its constituent amino acids. We want to know the chemicals and conditions involved, the mechanism, and why 316 process works. {a N M‘ HOOC.’ Nun'qu *2. + (fie—I'd“ “7,0 M Cow": when “'17:?— \ 0‘; curd» 11m. 0Lch “H m. *1 .- -. H i (“dim b ~MMICA‘M‘Mj th 53+ cake? £‘H 4’5 a“ M cubmfiz making 3+ 4; bet-lev- , , . m _ cl MR H 0 . (5 pts.) c) When the ion exchange column 15 done ringing, we nggce The resin bed is smaller, i.e. it has “shrunk”. Briefly explain why this has happened. A-‘r m “J. 4 W wwimxd” flu. 501* mmfiafim 35 higher! i.e- 6.36 [J (M M 0’2 5.), m 5AM m resin beau. «liminj {40:241. Affflabk M 0W, M rein-455.. in \ D - w shrinkinj, é“) _.. Sku- g 3 50;. - 3 0‘35 .0; 20f3 BIS 102 Name 2. (15 pts.) Explain how the following two images relate to this part of our course. What are the images referring to? How are they different, in terms of what they are trying to explain? What are the various items that each is trying to get across? r ' M‘ ‘ a. 410014 +5 I. 90%» 3M as "it" +1: QM £v\&\:3I 3am!) gram" M“ random “'D" 4-; MM. mar-Eve 3 a,th N , I . \ \ z m than? M 44»; “lwfi‘l'ro-‘rlad. ‘HA-fl— (luau-m 0' HJV‘A‘ ' 13¢ fiwl 3-: 9M Cw‘QANmarhm cJawim were. re hQ. a» 446:? phwa. “(‘44 ‘ls inrA‘ kw QM cal . “YMM- vMAM W“ 41¢“, Jean \Ma (cull/t +u alum. VHF-4— 3-2» “MMM fir—Hm M Nagy . HA1 47.4.1“. (racy-*5 v“ "HAL We; 9:0 ‘ in. m +5 3 fi—wl 2"__, ‘31.. “Mix 2:2“ a? fiumdfimefim prologue. 3d- kapd in a mks-€le , 3. (5 pts.) the main take-home message of a Ramachandran plot? Moot cb, xv M3244 m net Mmmo a MAL find-twat, 4. (20 pts.) The proper functioning of hemoglobin requires an exquisite balancing of weak bonds. Carefully describe these weak bonds, in detail. What are they? Where are they occurring? How is the “balance” physically communicated through the hemoglobin molecule? What amino acid residue, in each subunit, is most critical for this physical communication? Why? 4. +5‘ l‘ defile bum:ng 41" HM?— W MC- 0; blwéb‘m +0 How. Feziw *Lt. km W O; \oimfllnj +1: 4M £25411 Mal-t3“ . +5 7__ m voted: lat/“AIL oegos‘mfi flaw. in H—w fil QR.— ‘HAL o-Q?Wlméfibj \75 +/- \Mt— lwa/x (5di— kriaég/Q cowrivxs MM MA wiA—M 44w. 30M- sfloauxifi. “I’LL “Koala/m4.” loch/vans Ham/>- 4“ M “'2 i5 Murich ‘HAYU'VJaJN m l-Ho moleQJLL bx) Mu. QWQQ MM 51.. VL—W (\W W)! W. UVHMI AMA 4"“ 1:61 Lg m W. +5 1+ “(LII arm‘mo M29 «51% M is Q‘Aaal {3 M ewflm‘fl hits-RM. 1* HMQWQSL WM \HMM +5 3. 3 of 3 BIS 102 Name Kg; 5. (10 pts.) A protein was completely digested with trypsin and an internal peptide (i.e. not derived from the N— or C-terminals) was purified. Determine its sequence from the following information: a) A» 0' amino acid analysis yields one mole of E, T, P, A, W, F, K, and R per mole of peptide; b) treatment of “49/ the intact peptide with PITC, followed by acid hydrolysis, gives PTH-A; c) treatment of the intact peptide with chymotrypsin yields a tripeptide containing K, T, and E; a tetrapeptide containing P, A, F, and R, and free W; (1) the tripeptide, in part 0, yields PTH-T after reaction with PI'I‘C and acid hydrolysis. Answer: A’K”P’:’W"TrE'-K 6. (20 pts.) The ability of pure hemoglobin to bind oxygen was studied in a cuvette, as we discussed in class. Using the axes below, carefully plot the expected oxygen binding curves for the following situations, labeling each curve clearly with the letter of the situation (i.e. a, b, c, etc.): 100 % 02 bound 50 0 r 24, p02 (torr) 100 Situation: a) Hb, pH 7.2 b) Hb,pH 7.6 cc; {L091 «Hm mm_‘*°. . x M n33”, but \H \omAMj M “we n . t a“, Wm, c0 b: ‘ 44.... same Wei—a c) Hb,pH7.2,75%saturatedw1thCO 3 it? Njww,”L rim “3 “6.” um)?“ H‘ 3&5 . OL— Sw‘ovudh. dul‘Lim 25-9,, 0... d) Hb, pH 7.2, 75% saturatedwrthCOz 444' 5—643" (L L e) Hb, pH 7.6, but the C-terminal histidine of the B—subunithasmutatedto anM e M m m t) Hb, pH 7.6, but the C.terminal histidine of the B-subunithasmutatedto anM sam— WVe5 and the N-terminal residue of the a-Sllblmit, normally aV, has changed to anL Q key Nr-i-ctmbwm ‘m inc». no all-{4‘6" SimLe, Hahn | ,4, mm +3 + K “M3 1 83>(e\= ‘5, F”. a} H»:- N'J-cxmnm \‘a +91 v-N'l'lz Draw, :23 3 2‘ 3-9%,“ (‘7 J1 Han. Q—cy‘owQ. c,wa 3‘ *2 ...
View Full Document

{[ snackBarMessage ]}

Page1 / 3

BIS 102 MT2 Summer10 - BIS 102 Name< Summer 2010 Last 3...

This preview shows document pages 1 - 3. Sign up to view the full document.

View Full Document Right Arrow Icon bookmark
Ask a homework question - tutors are online