Class Note for CHEM 490 at UMass(21)
Class Note for CHEM 490 at UMass(21)
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This 21 page Class Notes was uploaded by an elite notetaker on Friday February 6, 2015. The Class Notes belongs to a course at University of Massachusetts taught by a professor in Fall. Since its upload, it has received 17 views.
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Date Created: 02/06/15
Protein Function binding Ch 7 Mon 22309 02binding proteins Heme cofoctor39 protein tunes chemistry Myoglobin Monomerquot 02 storage Hemoglobin tetmmer cooperative binding 02 transport Binding equilibria YboundtotolMbOZMb02NlbOZOZKd binding cur39ve V vs 02 affinity hyperbolic single Kd identical and independent sites sigmoidal multiple not identical and independent olloster39ic protein Alloster39ic effectors BPG H CO2 Sickle cell anemia Protein Function catalysis Ch 89 1 subunit so a 009 HisZ Yfractional saturation O P on P 3 h P N 00 Pure hemoglobin TISSUES no 23BPG Lungs Hemoglobin in red cells with 23BPG 020 50 100 p02 torr 150 200 a 0 Fetal red g ed 03 Maternal hi 5 re ce 5 993 H 34 E 06 s y Tu Pa 5 M w t 02 flows from maternal y E gt 02 oxyhemoglobin to fetal T deoxyhemoglobin I 03900 50 100 l l p02 torr CT R a g s h 52 2 MRSM E A 3 08 m w 3 E 06 In k g 04 aga E 02 1 139 If gt r quot u quotquot 00 0L 0 rigm 74 a simmrm Sixm 5minquot A was w HFluemun and Cu Tissues munnv 100 a2 Lys 40 wunquot AM Cterminus Added proton B1His146 9 B1Asp94 ragmuqs SLQF5 T m Binrhzmv39 ry Six m Edikiun muqu w HFleeumlland cummy Bode tissue Blood cvapillary ngm no ummmry um 541mm n Jousw mmn mumpw J R O R 9 4L N H lN C H H o quot39 b Curbamufe mm um m Prorein Function ca39ralysis Ch 89 l FNKFWQ Enzymes ca ralys rs amaznng ra re enhancemenst No change in equilibrium How Binding general chemis rry specific Enzymes bind subs rra re kine ric curves maximal veloci ry Enzymes s rabilize fransi rion s ra re MichaelisMen ren kine ric equa rionscurves KMI VmaxkcafEfof kCGTKM ca raly ric efficiency perfecf enzymes diffusion limi r Inhibi rors Transi rion s ra re analogs Irreversible inhibi rors Nex r chemisfry specific mechanisms cokm MAMquot TABLE B I Rate enhancement by selected enzymes VquotWW Nunenzymztk Unnlilyxed me cmlyxed ale ne enhancement Enzyme halfllfe lklmsquot kmr Ik squotkunsquot 0MP deuvboxylase 73000000 years 23 x Hr 39 u x Inquot Snphylnmual quotmm 134mm years 17 x Inquot 95 55 x 10 AMP nuclmsidasa 69mm years m x 10quot aa sn x m Cavboxwemldase A 73 yeast 3 gtlt Ioquot 579 19 x mquot Ketnslemld lsomemse 1 week w x Inquot 66n u 39 x mquot Triasa phosphzla isamerase 19 days A x 19 43nn 10 x 109 Chonsmam mumse 74 hours 25 x 1075 50 19 x m6 arbonlcannydrase s suonds 13 x w l x mA 77 x w Abbreviations 0MP ovokldlne monophosphale AMP adenosine monophosphale 5mm Am A Ridxkka and n anlndenJa39mm 26719959n93 Table as Siamvath sum Eamon gt2uu7w HFleemnnand emumy Mead oc rim Sij rasm de Stain Couple vpA1AMAL ov39slw 3lt Spec I Free energy G W w l r5 Jim Transition state l W ar Reaction co9rdinat 6 55 M tRTQdeA Product gt Enzyme 3m via 35 No enzyme 9 olL W x W MA J II Seconds Hours Time gt rigm as amnmrm quota mm w m A B N 51 E56 a No enzyme LE s gt m 5 5 0 5 w Substrate Transition state Products 2 metal stick bent stick broken stick quot39 b Enzyme complementary to substrate U Magnets E o G v 5 3 G c Enzyme complementary to transition state Free energy G t 4 l quotI l I gtI I ml l l I n I l I quot39 I I I I I I l I I Reaction coordinate Lehninger Reaction Rafe enhancement CI 0 H g CH3 C OR OR CH C Lgt 3 o 1 kM s391 Cquot CH3 C CH3 C O quot3 39 QM b o o 3 MW c on 0R c 2E 7L9 5 s39 ve c o c a r g g bb CNCA w c 0 o 0 0 V 3 cm i E s 10 M I k 5quot gt0 53 8va c o c Lehninger o max 2 max Reaction velocity V0 gt lt I I I I I I L Substrate concentration 5 gt gure sq 2 simmmvy sum mm m wu w Hrmmauu mnuuuy Vmax Region A gtgt CM V0 v0 kcatE1Lyfo Region B 539 ltlt KM v km E1S1 0 Km A S V m CE km Region A ES gt E P Mm quot39 K V km RegionB ES A EP ES gtES gtEP Figure 55 Principles of Biochemistry Me 2006 Pearson Prentice Hall Inc Intercept f 1 E LineweaverBurk equation 1 Km gt 1 1 v0 Vmax Vmax Figure 56 Principles of Biochemislry 4e Vk4amp3 V M5 Avoid Scatchard Lineweaver Burk and similar transforms httpwwwgraphpadcomcurvefitavoidinearizinghtm U1 0 9 0 2 A 2 E 530 L5 9 c 320 030 1 0 10 o o 0 so 100 150 0 1o 20 00 no so 60 Bound x 3M24M I KI HE Baum BUJnd
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