BIS102 Final SS09 KEY Hilt

BIS102 Final SS09 KEY Hilt - lof2 BIS 102 Name % Last First...

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Unformatted text preview: lof2 BIS 102 Name % Last First Summer, 2009 K. Hilt Final Exam Score (200): Equations: pH = pK. + log {lbllial} K. = xZ/(y-x) Kb = x’/ (y-x) pH = (pKa, + plug/2 (K.x1<..) = 1 x 10'“ F = (q‘ qz) / a :2 AG = AH - TAS v., = {v,.m [S]}/ {Km + [3]} Amino acid pK.’s: a-cmboxyl group (2.1), (at-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) 1. (25 pts.) How many moles of HCl are required to change the pH of 300 m1 of 0.200 M histidine buffer, pH 9.8 to a final pH of 2.6? Assume that addition of HCl does not change the volume. Put your answer here: 0 - l I 1 mols HCl. To receive credit, show all of your work on the back of this page. 2. (25 pts.) Crystals of deoxy Mb are stored in a N20!) aunosphene. H023) is added, nothing happens to the crystals. However, when crystals of deoxy Hb, stored ' Nm are exposed to 02(5), the crystals shatter. Explain what is going on (i.e. “Why are the two outcomes different ”). Give a detailed answer. Binab'wt) type 57 [/6 +rlj a. WM FL Fe"1L ,‘wl-a “Ha. glam-— if. (Lg +5_ emfhjvin final: #14 5 MM is +ramsij-e1 firmj/{N M emimd “453R - . 1 4—K I a :1- 0“ de‘ngW armé.’ rMM-H-inj in & hang—,5} 4,. "x H49 3 m2 I-t 5WLL¢M L W Lye-445 541. LA‘QZuIA-S a All) notch 0"th tic/<44“: ,‘K ML. 3.(20pts.g200mlof0.600MNH3ismixed1' 400mlof0.100MHCl.WhatisthefinalpHTl‘heKbofNHgis 1.80x10'.Putyouranswerhere:pH= ‘7. G .Toreceivecredit,showallofyomworkonthebackofthispage. 4. (40 pts.) Chymotrypsin cuts on the carbo ‘1 side of aromatic amino acid residues. Draw the active site of this enzyme, using chemical structures (you do t need to draw the substrate). Label each part of the active site. Explain briefly what each part is doing during catalys s. Points will be given for the clarity of your drawing and your explanations. 1 *1 KM 9M Qa£¢°Hj avievd‘s' sodas—Hail, ‘ Q auxin-M61 cum 3!»! 0;ka L.3 3"”. +3 *5 (arm-P can‘ton posit-CM) I ‘M\\ \/¢_—— cHz— HS} lam (“537.3% ‘HD C” c— 43 l a T S H’ - +3 "is- E/H Jed L": o s? 0 nulls: lg ‘/ I Miser, eKa ,e' {4.5,} +5‘ fl —\' 4.6 C‘J'iz 2. +2_ 5— fig + b 3 govwxs 5W H~~bmA “EM. 957 l0}. Min €0.00 ’61 M wmfiwm 20f2 BIS 102 Name is 5. (40 pts.) In class, we discussed three types of reversible inhibition that occur with enzymes. In the space below, do the following: 1) give the name of the inhibition, 2) write the chemical expression for the inhibition (i.e. E + S 6-) etc.), 3) draw the diagnostic Lineweaver-Burk plot for each inhibition, and 4) discuss the binding site for I in each case of inhibition (i.e. “How is each binding site for I difi'erent7”). fl, 1 cam'om-NL t A‘L meikw 1:- ”" Vtanth ‘3: E+$flzsaé+9 +3 E+$2€s-g+€ *5 E+sg ss—a €+P +- + a» + I '1: a: r 1‘ *‘ t’t >5 tr if t J. E‘r Va 4; 55‘: En: +$ 3551' "" )Jv t +1: 3 *3 *1“: T #3 ‘37:: n, f A' 3.. L51 3. g 3.57 _\, j: bhflfls M S 4’; it 5 Mus ' t f A H's W MIT“: AM. 6' sfl-e, @w I 4'; ‘:H‘ *5. 6. (20 pts.) Give theWanddrawthe Mofthe aminoacid, inthe fonnthat ould predominate at pH 7, that best fits the following descriptions: a) this amino acid is why B-mercaptoethanol is added to protein solutions C—H J¢H1_ SH w b) this amino acid gives the smallest peak in Edman protein sequencing, due to its nucleophilic R-group 5 4" —- ellz— OH H! c) this amino acid has the most (11>, ‘1’) values possible in a peptide 6 +\ _H Ht CH3 1“ C d) this amino acid is the most hydrophobic L“ _ C“? L“ _, (93 or . c _ L - <, 7. (30 pts.) Affinity chromatography, sizing columns, and preparative IEF gels are all techniques that might be used to purify an enzyme. Do the following: 1) describe the basis of each technique (i.e. “How does each technique work?”), 2) rank each technique from best to worst, and 3) explain why they should be ranked that way. A fiiinikt} iEF 345 S; viva “AW,”L (“3 +5 \ 1 3 ,' biola‘zjlcé s‘cffs—icifi ' «1' 4'5, 52:;- M‘ '14- m mdwlv flirm “6mm. zB wawismli%hw~£€WfTM%’ ac WO‘MJL I,3°¢L/Os+val-w€ (OJHMI/ M a. sih."° ‘u I 'w; “W WWI re aim. Hm. hurt 1mg .‘22.; MW}?)A%¥3 \ TL) “*3 "3 5t“ HL’h‘cfgé -mwm - > h . W 3* l ' .0 ié I '4 "’ “f” f? _7 g —-> W“ W“... ..__._,___‘C__/___A1L.____.,..___ V W C. w ____ W I mn~ii_:21f_’_________:w a a “W I H i _ ......... .m mm. .____'t__ ‘ I fH?-2. _ mum I J 3019 2 020,1 1V4 : 4, 0&0 Me M4, _ ....... W m.ww7___mmw_WWW 7 La. mm 0! Kurt (e = e¥~+ (33 g: _ .1.» 2.14- #— q.?=¢1.e+ , _ “ m 4.5: I h— 0.2. s )5; 3L, m . é= - a= — mu A: 2~ ~ , I a VJb " ‘ 1 ‘- 2.5'? I W l Ida! 4. “Jud-s = 4.23 4— I + a.“ m. I WWW WW I /. 95 0.450 nut tw‘a = 0‘ u/ rut-C H" V . ' WWW—m I 3. v.2w ,1 0.1.4» M NH- : 4.12 .1 N V 4w L 0.11m M ya = 0.0»: Mine” WWW K 3 Lioxtd L : (7‘10 n Kc» = 5’ X» J. K a: 9,2 _ __‘__ Ill 2 Kg. '1' / b M 0-0? "““‘* mm: W a 7— 41.2.4. + o,'30 a: 7 56 u WNW, .u w ,W , V’ ,._._..._,.. ...
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This note was uploaded on 10/22/2010 for the course BIS 102 taught by Professor Hilt during the Fall '08 term at UC Davis.

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BIS102 Final SS09 KEY Hilt - lof2 BIS 102 Name % Last First...

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