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by: martinlutharking

Chem109CMegaFinalAnswerKey2013.pdf 109 C

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Organic Chemistry
Paula Bruice

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organic chemistry 109C paula bruice mega final answer key
Organic Chemistry
Paula Bruice
75 ?




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This 62 page Bundle was uploaded by martinlutharking on Monday October 27, 2014. The Bundle belongs to 109 C at a university taught by Paula Bruice in Spring2013. Since its upload, it has received 110 views.

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Date Created: 10/27/14
A De ne I Anabolism simple molecules energy quot9 complex molecules Catabolism complex molecules 399 simple molecules energy Apoenzyme enzyme with its cofactor removed inactive Holoenzyme enzyme bounded to its cofactor active Peptide bond the amide bonds that link amino acids of a peptide Glycosidic bond the bond that attached the OR group to the anomeric carbon in the acetal 7 Anomeric carbo11 the carbon in a cyclic sugar that was the carbonyl carbon in the straight chain form 8 Competitive inhibitor a compound that competes with the substrate for binding at the active site i 9 Suicide inhibitor a compound that inhibits an enzyme by taking part in the p normal catalytic mechanism thereby killing the enzyme S 10 Nucieophilic catalysis cozvalentseataiyzessthcreaestionwbyfmal ingabetter p f L J nueleopihsile Mitt IMa 53its it 5 Mic rr 22 quot tquotlt irt zraow 56 5 gt 39 Q 2 c 3 5 r v Z t3quotquot39m 5 11 Cofactor a metal ion or aiiichqrgaiiiic molecule tha an enzyme needs In order o carry out a reaction 12 Coenzyrne an organic molecule needed by an enzyme in order to catalyze a reaction 13 Vitamin a compound needed in small quantities for normal function that the body either can t make or cannot make in sufficient quantities of 14 Electron sink a site to which electrons can be obtained 15 Dehydrogenase an enzyme that catalyzes an oxidation reaction 16 General acid catalysis proton donated during the slow step 17 Speci c acid catalysis proton donated before the slow step 18 General base catalysis proton remoyed during the slow step 19 Speci c base catalysis proton removed before the slow step 20 Endopeptidase an enzyme that hydrolyzes or cleaves or peptide bond that is not at the end of a peptide or protein 21 A disul de SS bridge in a protein a covalent bond between nonadjacent amino acids in a protein 22 Primary structure of a protein sequence of amino acids 23 Secondary structure of a protein conformation of the backbone of the protein 24 Tertiary structure of a protein 3d structure 39 25 Quaternary structure of a protein arrangement of individual peptide chains of a protein that has more than one chain 26 Fatty acid carboxylic acid with a long aliphatic tail which is either unsaturated or saturated 27 Lipids naturally occurring non polar molecules quotquot E9 B Answer the following i i 1 intermediate formed when RG00 attacks beta phosphorus of ATP An acyl pyrophosphate 2 What coenzyme provides the methyl group for thymidine N5 N methylenetetrahydrofolate 2 3 Other than the substrate enzyme and coenzyine what 3 additional reagents are needed by a reaction that requires biotin as a coenzyme ATP Mg2 HCO3 Q7 Mi lkxco C 391 39V1r fi lt 339quot27 w 39 a MA 9 l O r l LWW5 xiC 3 ivg Ki mr 1iV 6 K 5 39 39 IS 5 3 I Equot 39 t i is 0 v1 6 0i39a 2 Afr ass i S I g quotv c L xx aF1Ve coenzyrnes that act as reducing hts I A NADH NADPH FADH2 FMNH2 dihydrolipoate b Four cofactors that act as oxidizing agents NAD NADP FAD FMN iipoate Aspirin inhibits the enzyme cyclooxygenase by Way of transfer of an acyl group onto the enzyme What amino acid is modi ed serine Which fatty acids are least likely to be found in nature CH3CH2oddot39carbonsCOOH What are the functions of FAD and NAD and in the pyruvate dehydrogenase system FAD oxidizes tiihydrolipoate to lipoate NAD oxidizes FADH2 back to FAD Which heterocyclic bases are contained in the coenzyme system NAD and NADP Adenine and pyridine What is not true about fatty acids The double bonds are conjugated What about lipids classified based on chemical reactivity Inquot the sense strand of DNA below what is the sequence of the bases in the complementary strand What base is closest to the 5 end of the complementary strand What would be the sequence of bases if the sense strand were transcribed intog1n RNA 39quot M 2 10 Sense 5 ACCGCTTCG3 Complementary Strand 3 TGG C GA A G C3 C is closest to the 5 end of the complementary strand mRNA S ACCGCU U C G3 1 1 How does the catalyst affect the reaction mechanism in the iodinecatalyzed formation of alcohols from alkyl chlorides Changes an SN2 reaction to a sequence of 2 SN2 reactions i lntramolecular reactions are faster than their intermolecular counterparts What factor is mostly responsible for this Great number of collisions between the reacting groups ls metal bound hydroxide a poorer nucleophile than water False Co11j Ligation raises LUMO and lowers HOMO the energy of what molecular orbitals r Enzyme catalyzed reaction that requires vitamin KH2 as a coenzyme What is the purpose of the coenzyme in the reaction To give a strong base that can remove P a proton from the 7carbon Whatreactionit111 uuratedehtdrogenase tliat hasquotco39en z yIn e A as ar139eaetant How is biotin attached to enzyme It is attached to a lysine residue side chain in an amide linkage 39 How is biotin bound to an enzyme side chain As an amide with a lysine of the enzyme What is the 3 monomer segment of a polymer that would be obtained from the monomer CH2ClIF Would it be better to use an electrophile ora nncleophiie as an initiator for the synthesis of the above polymer is the above polymer a chaingrowth or a stepg139owth polymer A W 3 s Pn 5in lt arrt Eva xfivI P z y II Iquot x N 39gt I w J Lift 54 y 3 2y z iibKig i ftj1 7 12 13 14 JI gr I pg L P3 393939 39 r39 J 39r3939 39 393 39 V5 W fSavzo vto939b i v I I r 5 f Aquot 0 I i ii C1Hi l iei r 39tiii39 quotii Vfi 0 g am In P j is M lr1 ti trt ri 39i it 0 F P A K 2 rjquot ti39 5 iquot xi 39 o as lt4 quot 1 l C W 0 D G J N1 6 0quot 7quot 7quot 391 0 an 1 K it T L M 39 s 21 Mgi 0Z ii i mi U i 3939f quotqi I C r fr 39quoti 24 ign iquot 3939 rf elt i A rquot 39 Eaquot Z 1 ib39e lt4t cu uti i1lt ar quot39 quot K 1 e F 9 20 What is the 3 monomer segment of a polymer that would be obtained from the following monomer HOCH2CH2CH2CH2COHO Q ll HocHcHcncncoH O c e4391ct i U 51Cfi 1j2 o ctLJcxts tiiE 5 CJllCf Which would be made with more highly branched polyethylene beach chairs or beach balls Arachidonie acid is a saturated 20carbon fatty acid How many moles of 1nalonyl CoA are required for the synthesis of one mole of arachidonic acid 9 How many carbons are in a prostaglandin 20 How many carbons in a monoterpene sesquiterpene dite1peret139iterpene 10 15 20 30 J i What is the structural difference between a fat and oil An oil has more double I c bonds than a fat 3922 23 24 25 26 has or16branches What about amylose and cellulose Amylase has u14 linkages and cellulose has 3 14linkages What about glycogen and amylopectin Amylopeetin has less oz16linkages less branches What about cellulose and chitin Chitin has an N acetylan1ino group at the 2position unlike cellulose which has an OH group What is the difference between a nucieoside and anucleotide A nucleotide has a phosphate group nucleoside does not 28 Which amino acids have the lowest aspartic acid and highest arginine pl value 29 Which are the 2 most nonpolar amino acids Leucine and isoieucine 30 What is the pl of arginine 1076 What about glutamate 322 Aspartate 298 Lysine 987 Alanine 602 31 Which amino acid is not optically active Glycine 32 Which arnino acid has an R group with a pKa 6 Histidine 33 The u aniino group of which amino is a secondary amine Proline 34 If 2 amino acids have pl s of 62 and 64 which will be closer tothe anode when chromatography is done on aquot solution of pH6 35 Which amino aid methionine or phenylalanine has a greater negative charge at pH620 i inethionine pKa s 228 and 921 ii phenylalanine pKa s 183 and 913 I What number of hydrogen bonds in the base pairs 2 inTA and 3 in GC 2 Identify the one codon that doesnot code for vaiine GCA What about leucine CCA second letter differs What is formed by polymerizing propene under acidic conditions 4 Which base sequences would be recognized by a restriction endonuclease L ACGCGT 27 11 39quoti lt 3 xT139 V56 Si if1J ft What is the structural difference between amylose and amylopectin Amylopectin 9 L E i6 C3 p areiii1 6L54C J 5a ff P to3 Lrp39i I 5l3 I 3939zif39i39hrt3 t b39w c IMt r ir rr M rquott73 tii r Vt ari rip WglP 2 1lg W3 LC quot f1r rag 1 ltquote39 ir gtcf2 5 f um ram y rr39W if Lo39ri 15 11u iejg t to 39 i39i gr ares eimegsae a strand read in the3 to 5 direction 6 A urethane is a compound that has which 2 groups Amide and an ester 7 Which amino acid contains an indole ring Tryptophan What about iinidazcle Histidine e 8 Which of the following compounds has the UV Spect139un1 with the greatest lambda inax ia 13heptadiene ii 1 5heptadiene iii 1356heptatriene iv 1 heptene v 135heptatrienc 9 Product of enzymecatalyzed reaction that requires biotin and whose substrate is 39d t lt39C9 7 9739 L It Cxidzxsgg 9quot quotquot0 C quotquotC 5C ll 10 Which substrates will undergo cyclization and anhydride formation fastest d Which of the following substrates will Undergo cyclization and anhydride formation fastest 39 W 39 ROOC CH2CH3CH2COD ROOOCH3 CCH3CH3gZH3CII2 C0D 13gocourCCH2cr gcH3 ROOCCHzCCH32CH2COO R0occII3 ccIi3I 1c1i2coo 11 2Thiosubstituted chlo139ocyclohexanes can undergo hydrolysis to form 2 thiosubstituted alcohols Which statement best describes the mechanism of this reaction for the trans isomer 12 PLP coenzyme is bound to the enzyme through what type of bond Through an irnine bond with lysine t 2 13 What role does PLP play in PLPdependent enzymes Delocalizes electrons l4 How many molecules of CO2 are obtained from the complete metabolism of one molecule of a 16 carbon saturated fatty acid 16 15 What does not affect the rate of a reaction The equilibrium constant of the reaction 16 What are the pKa s of the amino acid side chains L r D Qrnaan Isa syntnet1c1anr c39rvlIa1mo11u1ners are risen to syciiiiiesnLe iU w p w I p 18 What interrnediate is formed when 3phosphogl tog phpsphoglycerate c W oeinnc e eilghth reaction is an isoa1crizaiion 3p39llGpl1 gi Gt3i39t39lIi is cerivezjt il1ES Ii1il 1ti tti The estimate thet catalyzes this reiieticii l3as a 39Jhospha139al 19 What is the difference between transcription DNA gt RNA and translation mRNA Protein 2 20 Pyruvate is converted to which of the following compounds in the presence of oxygen AcetylCoA What about in the absence of oxygen Lactate What about under anaerobic conditions of yeast Ethanol 2l Chargaff measured concentrations of AGT and C in DNA What did he find lAlTl and lGlquotquotCl 22 What gases are given off when the tBoc protecting group is removed C02 and isobatylene 23 Which of the following is the main difference in the active sites of all the serine t proteases Size and charge of the pocket at the active site 24 What kind of sugar will be obtained when an aldohexose undergoes a Wohl degradation Aidopentose 25 Which of the following reagents is the best one to use if you want to reduce an aldose to an alditol N aBH4 26 Which tripeptide can be cleaved by carboxypeptidase A ProPheVal In what form with the carboxyl group and amino group of an amino acid predominantly exist at pHgt 1 1 W s 28 How many stereoisorners can an aldopentose have 3 t 29 The coenzyme pyridoxai phosphate is not required by enzyrnesthat catalyze donation of a onecarbon group 30 How is the coenzyme PLP bound to its enzyme in an imine linkage with a lysine residue 39 31 What is a dehydrogenase An enzyme that catalyzes and oxidation reaction 32 Which of the following does not contain a monoterpenc T pU U 52 ii iii iv v vi 33 What 1 Olive oil Lemon oil Rose oii Peppermint oil Juniper oil ole doesATP play in biotindependent enzymes It puts a good leaving group on bicarbonate 34 What is the common spacer between the CC double bonds in polyunsaturated fatty acids CH2 35 Which of the following waxes is the least likely to be found in nature vii viii ix x xi CH3CH228COoCH219CH3 CH3CH22lC00CH231CH3 CH3CH230COOCH22ICH3 CH3cH22oco0cH225cH3 CH3CH224C0OCH221CH3 36 The synthesis of which nonessential amino acid is impeded by the disease PKU Tyrosine r x11 39xiii xiv xv 38 In the cycle xvi xvii xviii xix xx 4 37 What is the second stage of catabolism Oxidative phosphorylation Fats carbs and porteins are converted into compounds that can enter the citric acid cycle Fats carbs and proteins are hydrolyzed to fatty acids monosacharides and amino acids The citric acid cycle metabolisin of fatty acids through Boxidation each passage through the removes 3 carbons removes 1 carbon removes 2 carbons divides the molecule in half removes 4 carbons 3 39 Which of the following does not contain beta 14glycosidic linkages xxi xxii xxiii xxiv xxv Chitin Cellulose Maltese Cellobiose Lactose 40 Ribose is the sugar used in RNA What type of sugar is ribose Aldopentose 41 What is the charge on the oxygen atom of the oxocarbenninm ion formed as intermediate in glycoside formation Partial positive charge 42 How many asymmetric carbons in the simplest ketotriose 0 and aidotriose 1 43 Which amino acid would come off last from a cation exchange resin at pH5 xxvi xxvii xxviii xxix xxx Asparagine Glutamate Lysine Glycine Serine 44 What alditols would be obtained if Dfructose were treated with NaBH4 following by H H20 i CH2 W c41zt i gJ usaid git VML R inirwer quot quot H lt2 H 39 A 55 quot tquotquot quotquot P Qybo 5 CA1 zso is 45 ls Quiana a nylon or a polyester C Explain 1 Why NADPH is needed in order to convert uridines into thymidines When P5 are converted to TS tetrahydrofolate is oxidized to dihydrofolate NADPH reduces dihydrofoiate back to tetrahydrofolate Why does conversion of each mole of uridine to thymidine ultimately consume a mole of NADPH A 3 Why DNA contains thymine rather than uridine C s can bedeaminated to Us A U in DNA indicates a mutation so it is removed and a C is inverted in its place If DNA had U s instead of TS C s that had become U s could not be distinguished from Us that were supposed to be there 39 4 Why DNA contains 2deoxy D ribose rather than Dribose The 2 OH group of ribose is a nucleophile and causes RNA to be easily cleaved DNA must remain intact throughout the life span of a cell to preserve genetic information Whyti a Does Not H are a There are two diiquotfet39ent39aitentatit1g grooves in a DNA hciis a tastier g1139iorc and it narroa39er uiieor groove Proteins and sea iaeiecales can quotbind to tire lgreeves Tiie iigltirogeihottdiiig progiertics of the In notional groups facing into eachgtt1ovc39dclen11iite Wi 1 i39E kind of m39oieeaics will bind to the groove lanes a1iquotpIe netropsinis an ehtibiotic that vre39rl s by binding to the minor groove of BRA Section 33 10 i39ntii c39ate sviletiicr each ineiio39nal gtoilp oiiito ne izeteneyeiic ha esi39n t1ueieieacids can fcnetion as 5 h39drcgcniioi1d acceptor A 15 hydrogen bond dcscrim erbeih Dirk Using the D A and Dir designations in Prcitietti iitdicate how i1 1E339 I3iI39itig s39r 2 1lii ite affected if the times existed in the chat fairs 5 How does 5 uorouracil act as an anticancer agent 6 Why do tl1e hydrogens of the methyl group bonded to avin at C8 rnore acidic than those of the methyl gzjoup bonded at C7 as y 3 E 1IFo z c e 39iv 5 quot39 39 quot quotL kifj him Vida y HCNNH J 6341 z p s ew J 40 zi 339 vquot 5quot quotquot lquot quot quotquot393 77 Cir 39 H1 7 The genetic disease PKU is caused by the absence of an enzyme What reaction does this enzyme catalyze to wuyuu Lnun ave I 3 quotquot 7 I cuCi1 iioquot Tl V3 Wr9 lquot quot p CCI 39 quot 54 Q3quot Iii 0 M E 39 t 3333 39 llo L 139 39 39i 39 K 8 How does a PLPdependent enzyme racemize an Lamino acid was ArcrtuInuno n v 39 1 y 2 cs quoti lJ 5 3939quotquot l 39 539 1 w H 63 quot19 Q1 Knew 6uo39i239x4lt quot quot W w W 43914 M gJ IL397 C14 av y 4L in 4lei g 395 z V l 424f4 2 i alga 3 P p Z Why does elastase cleave peptides only at the Cside of Gly and Ala jglii LLp c F 10 When 5Dglucose reacts with an acidic solution of ethanol why are the 02 and B r gab 2 glycosides formed 14 C quotqr l iv l4quotquot t 9 F ml an vctvg J 90 rm 39r Zwir39iiu 610big W9 quot nil Zoo r vs 395 W ampu1d ff 0 3 ikvtwlp Ed JM n m flmcl y sfjl Cf gtyfgt K quot 1ampjvc lllll V U H 4 C 0 Pee P Q 31L 4 cs N C zoL L ga1act0se C H 1 1vtf39 tr 3 139Aquotquot39 I 39 Cmpliv ozDgalactose oi5 ans 2 W OM Methyl3Dmannopy139an0side methylf D mannopyroanside c Mquot O r Ethy1 3Dglucopyranoside cAWquot i39 Wquot 53 Mamong an 7 Two molecules of Dglucose joined by an 11 14glycosidic linkage 39 W M W H6 as so 9 8 C3 epimer of Dribose C44 2 0 loP 39 jQ 6P i39 4quot Hquot M i g i C r 58 H gt cJ H E CUrua H z a 9 Dhexose that when oxidized would form an Efitigiilly inactive aldaric acid Ct 39to C4E ct I 1 Jrquot 4 it o IL 14 o Iiv 115 39 I4 own H 10 2 aldohexoses obtained from crystals of Dfructose in a basic aqueous solution Dmannose and D glucose 11 Sugar that forms the same osazone as i D n1annose39 Ci 4 H il 3erpiii i1J if w o Q quotJ ti39139a39 34quot iv I 3 iv B 4 0 10 l H is H me erawu W g rgg 34 O H 5 Jp c ow 1 f d quotWquot WLL 32 Q 1 Inix ii Dribose 344 lt3 gm H 49 11 5 4 C 1ot l 12 1a 9 I19rz1erS 05 q 61 Lej0 www C Cm quotquot I Ho f3 wa Ho 5 quot390 V 013 13 1yg1139 ducigg sggar M 39 HC9 Z9 I 14 A reducing sugar uxw Ub cm0 H 0 15 A wax e39 ii39 D i3 H i s2s1113 rm1vt1y a111m11cg3tquotm damp 3quot139Ai 39E3tf 39i sil 2 var39ax iii in 39Lf1 mr puIiIm E k I k a niaiittr 2 iquoti3 1 T3I iamp iE 9f 16 The stegpid ring system J I 3 caarrrea 27 he 39 tp 39cnt nr pyrcygslsmphaie tmilhe m canisn1 for its 13 as 93 1151 farnassyi 3 II39ijliS 17 Pu139ine and 2 examples f jhjj r7LEK lt N39 H KN quotH 0 0 M V 05 x 1 PU Jrwr J I 18 Pyrimidine 3 Examples Hw Q W 3 3 sgiycasiciig i 7 33 J a g gEycesteiI F1 linkagequot 0 5quot39Liir539ag 39 2 r H grgaup anom39nI 39 39L39sItwcv39 rm Draw lhgt slim11 393939 far m N 2 dCIP 2 I3 dTTP ii I 4 T I U U I U 2 H0 Cystine G I quotc 39ic 4 s s quot1lti 1 3 39lt J au3 4Mlvl 21 dive the structure ofhypoxanthine l j M Z w 39 0 1k x quot 39 quot 39M 22 Histidine at pH 7 4 and 12 a His dine is shown as it prederninatel mgi 3 DH 7 CCg i3HlI0quot W NH3 V3 39 Draw theetructue that predon nalees 2 at H 3912 1 1 at13II iisy if go P u JCMCJo g w w ilg k 23 Draw a deeapeptide that would be cleaved into a eta peptide a dipeptide and a tripeptide Se1t Glv Ala Lou Met Ala Glv Met Leu Met 24 Acetylcholine T 5 fquotquot3 C1g rmct 391c 4xo73C15 Q5 25 Pyrophosphate Pv Oquot 0 L H 1 P 9 yk U quotU quotU 26 Aey1Py139ophosphate 9 7 I It pM 39 39 39 c459o P0 tf 0 e L L 0 27 Phospholipid that contains choline 13ee1Ie5j ihe 1zajoremn1p e1e1 5 zdee ealled p e1osptiniipiei3 iipi is 3 ante similar to triacyIgiycere39I ex eeiti p31espiteie a39ei39dr2aeEeher 11 an wii ember ef g1 yearn neataaraeily ee39u39r Q C 1 R 0 p X lc l 3 L CH rRl cm I E 9 3 Iiw 0 3936I LIh iquot 1 0 AL J 28 Phohsgnolipid tI3ateo11tair1 ethanolamine 3939393939f39 39n J 6 quot 39W rquotquot 39rfquot399 J HJ 39 z all memhntaast belong to a class of t2i11 ifI 1lIE x F O entain it jswhosphate group Piljtttipit tt igE i39 0it I A 0 mi 1 tor39ni39nai 3171 group of glycerol is cateriiiedt I ttty acid fanning a pIosphatit lia acid The 32 F1 0 w P 12quot 1 gift L15pitotoi giyeerots has the R eeafigaratia11 39 D7 I 395 ll t Q p octgctt ottg a r i391g quotquot0quot at I L I Rso39nfia39uratioi n 0 29 Transamlnatlon reaction Give an example of a transamination reaction 39 0 39 0 0 If r 5 if A yr 2 9 E 91rC 0 aagwc c ca 5 a gp39cLc rHco bllb 399 399 39 U5lgt 30 Biological reaction that requires biotin as coenzyme e Give a bioioggfat reaction that requires biotin G 39 r cg g 345 4 p quotE3 c39Z S39C L 4 P 5 9 F c 3c CE39 a wc 5 cfe 31 A pHrate pro le for an enzyme that had one catalytic group at the active site with a pKa 62 that functions as a general base catalyst and one that functions as a taaaaxatasi eatalsaa 39 32 I ATP is deaxninated as o 390 39 quotquot quot er I D thanolamine 91 Below is the structure of FA D What is the structurehf FADII2 34 All amino acids E Predictthe product 1 CHO HOH 0u IIC r H 7 L W HC H OH Pn 9 o1 ctzoH 2 Ho II E 1 we 394 HObH 2 Ii2PdfBaS04 H 4 M 4 IQHl 39 3 H H2O 914 P CHEOH xwu 0i39z of 3 IICrO CJDJJF IrIO H B2 M19 1 I IO H H30 pr H H OH 07439 4 V CH2 0 H39 w I rv 4 HQ on CH3OH 390043 0 0445 5 HZOH 0 ow quotquot H 7 e rn iquot h 115 D I 91 O OH aH I M 0 kOC llCAlrb H 0 L wipukb as H HO 2 0 excess CHd U 4 H0 0 T 05 5 OH g3 CBc 7 V c SH 95 I E 0 cw scum Wa V0 H3 39 AIL 300 1 8 the rststep in t39hecitric11 idltycIe C 39bW 39 coo c r 1 39 0 C cu3cncaampo 6d s wcJ ampc JPNH3 12 Jmjg 9 C O O I 39 H PdC 2bquot 39 W SM OCCHLPi3SSCH2lHCO H g Mu NH NH2 a 10 NH Nquot i C9 E PK f gt deammution l R I I 1 0 om 3 E 39 3 9 3 zUgt 3939 H 39 ADP 3 iquot 0 2 g01 ATP H201 0q Z 39 4153 P03 quot 0 II I C H3CCfHgamp0 mun H M nae 94 Oz C t5 tl4gc3c 13 I V 39 H 9 3 1 o CH3 0c NH HCOH Fquot C43 lt H l 21 EH 5 awaw w M 3 o W 14 4 minutggi 10 paints 2 E116 products of the following reacticms 5 C20 1 HCN gm we 39 2 5 0 r4 Hmmo 3 HH2O 1 quot CHQOH J uh n I 39 r39zn 3 15 E H x x 2 mac 39 P C44 3 ctr 39 U D 039 39 quotquot04 0 Ho cH2H30 quotO2C2Cl2 l 0quot 7 quot quot3T39 quot3 5 2F 39 QM 15 NH3 J F Cf HIC Hl30 EH2 1 man CH on D Q 2 2 R e m 14513Jlt s 2 ICHZCOH 1 C x 09 C H2 O I H n HqIj39iHCO39 5 quotc quot C 17 39fjE3976quot AI I 7 0Hquot 3 NH NH wmug 3 2 H0H CL L 39JLJi3 Q H0H 739quot Ikc 1t a 1 H OII H m 4 hail bamp39 CHZOH 39 Wuia 39 18 H O 0 C4 C I 3 H ii CF3C0OH 1 r H CH30C NI IS2HC0 0 4 Cltgt 1 r15fl Ctb CH3 CH3 L V C45 19 CHc C4 3 H H 1 cENHc1 1 p Hg 14 H O 39 39 2 H3PdBaSO4 z1col4 NJ CH01I 39 A 39 9 2 Pt c M 20 L glgficegzldchyde 3pI1osphatc g 9 HC0 mar IIPof 3 5 ge 3 I 39 quotH H OH 14 cm D CI2OPO3239 mtg P5353quot CH HC 2 1 I 2 E 3 cu EH3 CH3 adj cw coo39 2 22 0 a Wjci cup an 30quot 2 HgfNi W3 23 c is Quiaria nylon poyesampe2 2 P Which the am are hiii1g39o2ihP2 1 2m mg rshyzrscir 139gcvu 1aJIn g g 39 quotI 39 22 ahd substimtcd st rylcncs are me anonomcrs nms cc ymcrization 39 a1ti Jn 39 ether ctmapouzxds can pniyxncri xndcrga lt Izaingraw 1 pcrtynzcrizaiion nmt39Eens 9 1 nIf nItih nnfwr m 7Ilinn avian539 11139 mi nrlirinir 24 2 E R 2 5 6 The iganlc Cfiemlstrj nfthe toenzymes Cor pnu ds DEIIVEii Iran hI39itan1ns irigf s 1 HN N H Hm s R G S Hg N I R R L 39 l391NT N I IN IN 25 mi lt2 2 5 N BH 2 g 39 a quot 3 2 5 5quot 9 CtiigfffrI mlt1quot39 quot1113 fggg mzg 24 5 P H E 5quot 26 139 33 it 23 2 2 ems 2 E 0Ts 2 gL egifg i Ifo a c 5 5quot j iT1 e1 27 c Q CT quot 3C3 QE3 1 gq3Bf gfr i bs bs L 3ITt739i355i 3E 5 I 3 9 39 J 28 3 2 s I L 1 W 13lt39cfL 6 e pq quot 7 39 3quot iJE j Q i f39 J 333 143 29 C33 Q cs lt5oc11 Cflliig lie g NquotIlt 3li JB f ltvgr 4 H JEg vmy r r mg 4 lt s1lt31 lt2 39 Cg 39 P a g 3a 0 1 ra if39 L gamp amp 5 b j bb H lt quot quot 6quot 30 53 P F EnzymeCoenzyme 39 EH3 3 39amp1 B 39 I CH3CHEHCO 390CCH3CH2 C0 quotW CH3CH ICO OCCH2CH239HCO NH339 A O O NH3 1 enzyme valine anlinotransferase coenzyme pyridoxal phosphate H E I It 39quot39 0rY 2 ATP Mgz HCQ3 enzyme acetyl COA carboxylasc c0enzyn1e biotin ff E CH24COquot quot lCH24C039 SH SH 8 S 3 7 enzyme dihydrolipoyl dehydrogenase coenzyme FAD G Givelnecllani ms O O 0 It 7 h It I 0 u u 9 CH3 C4 1 I Based oi 0 HO OH Base2 2 HOH 3 c I 3C39B H mg 3 9 an CO2 e on gtLE gt r 55 quotquotquotquot E3Q H H3 C4 u L H7 an 3 05 4 3 lMs 39 3 o The foliowing rcoclion occurs by 1 mechanism involving generaincid catalysis Propose a mechanism for the reaction b The foiiowing reaction occurs by a generalbase catalyzed mechanism Propose 1 mechanism for the reaction if 5 o C UCH3 K o L CH30quotH can 39 9 a gt Give tho mechanism for the foilowing reaction we t l I I ClI I 2 C52 H fl 1 9 CquotquotN iii P I quotquotquot39 quot39 H quotquotquot quotquotquot39 quot quotquot r Inn up quot3939 nnu N CH C NHIC 239 H20 NHCH C 0 NH3lHC R R yon do not have to show the rnoch anism for mono hydrolysis 39 my bus 3 3 C143 E1 M2 10 12 Acetolactatc synthase an enzyme that catalyzes IFI6 I llowmg Icactluu ruqutws umiuum pyrophosphate Propose a mechanism for the reaction Note that the reactinn uses two equhmicuts of pyruvatc F11 enzyrnc has whatesvcr H8 or 839 groups you might need to aid ihe catalysis 6 0 o 39 0 OH O p 2 3J3E Ll flquot nu Cl13C1 80quot C02 B we 1 Km 91 gig ltgt1 3 Q C 5 0 015 CEIJ E i 7 r2NFJ H Ia A S thiarnins pyrophosphate 1 3 Hlt13 C a 5 5 3 otrg33lt5 E P E Qquot5quot1rpi C1 clt1 i1W CL C quot39 quotquotquot c lt 3 lbi 5 e w 5quot quotquotquots 639 1 C E3 r U39 39 5 zw 5 1 1 dug A carboxylic acid can be activated by an enzymacata1yzed reaction in which the carboxylate ion re ts with A EGive the mechanism for the activation 39 o 9 0 o 5 I 0 I O 2 D 0 0 I 639 quot 0g 6 lt5 quot o o 39quot f x Z2 2 Using arrows show the mechanism arrows for the first step in the mechanism for chymotrypsin IIi57 fefws 0 CH2 EH2 R 4 ll 39 L ASp1g3 CH2C0 39 HNp39 N lfirst step Hissh 37195 t CH EH3 I gt K H A3P02 CH3C0 0 a R 0 a NIIR a What kind ofcatalyst is histidine in this step eA2AaLQ m I What kind at catalyst is serine in this step 0 Y c How does aspartata catalyze the reactiun 39 6 39 5314 2 Give the mechanism for the following enzyznscatalyzed reaction Start with PLP attached to tha enlzyme as shown and and with PLP auaqdted to the enzymc You do not have to show the mechanism for transimination just write transiminaticm over the arrow 0 O 0 ll 1 I H H30 I 117 ll CH3lLHC0 GCCHZCHQECO w CH3 C0 OCCHZCII353HC0 NH 39 0 O NH2 Using arrows show the mechanism axfrows for the first step in the mechanism for chymotrypsin HiS57 r195 CH2 ifI2 R 4 I 39 L ASp g239wCH2COquotquotquot quotHN N m qt l rst step H1357 ff39 95 a What kind of cataiyst is hislidine in this step 224I ltaQ 6 a an I What kind of catalyst is serine in this step c How does aspartate catalyze the reacticm 39 539 J1 L369 n x uu 14 Give the mechanism for the following enzymecatalyzed roacti on Start with PLP attached to the enzyme as shown and end with PLP attached to the enzyme You do not have to show the mechanism for transin nation just write transimlnation over the arrow 0 II I HOA Ii ii ll CH3EHC0 occ gc gltltrco 2 w 39CH3 CO OCCH2CI2fl3HCOquot NH2 L o 0 M12 N HC t V u N 05 H quot quot cf O I Cquot3O HCHECHZCHZCHK scoA RCHQCHECH cuquot secs 1 H20 L OH 539 Z ukb 5 1 W urn 5 0 CDASH 0 O P I H A c C c M CH gem J RCH3CH CH2 saw 15 i What is the first step in the reaction cf the substrate with coenzyrne B32 in an enzymecataIyz d reac on 1 1t quires cioenzyme B12 39 4quot quotc 15 65 e4 c 3 7 4 S1Li d cJ 395 L 5lampLmcltJ 4af4quot4 r 17 Dez I16 ue foilowing nucleophilic catalyst W 0 Iz z sf2ltf i 5 gb x 7f 01 9f quotE39 3 fgir39Eag b a glycosidic bond A W 21 i 5 K I2rUs1 z9 E i i53 quot3955 c ter1iary siructu1e of a protein rquotz 30 I 1rtL5quotinse 4 ii p 3 cm zisa 214 39W E 1 8 E 1eJa e sL 0 0 0 L L g39 p3 n k 0 C 3 B h V V st J as2 39l1ji39Lit39i 2 Li 1 i39Jii Liii j if i iii 3 IEfS quoti7 r u j1L1Fi L1 2ie39 i a HO U I I I P 39 o t I I I N I I H I H H e x I I 39 H 5 I W p LX s E 39 39 I I N I R 1 r rquot4 in L 633 20 i M Ia st 2is1i 1 si i3 gi r4 x j LieabaTIfatiL iis vEiVi vigi 12 3 iVit3 39 AN P wO Q J x 21 M N O F p I UK V P y L an 64 ggi2V1i 4L I I I N K H P K p3J An3393sia239 39ih iii39 amp i9lg1 39 395 a39 5quot quot C xm iE rAmzrs Vmrmzsriie s2 ig Ii 139II1 r 9 i1 i39ClIgt2si2tag 1w1gtL1r2i 39 v1i12 LI11 f I f ii3i5 iT33 m 39i5 39i i3 Ii 3i i3 39 i39iP553 F 39 3 EH3 iiwi f 5 quot s ul 391fa I am39 z3ir r s Pquot 39s 22 E G I 3 Glu quot quot0 4 H CH 011 H 0 4 H is C39 H quotHis Q L w 39 HiOH 2 2 IJHZOPO3 P HZOPO3 dihyd roxyacetone glyceraldchyde3phosphate phosphate 39 dehydrogenase O Ga Ev oggbtlfrfamp p K1 Ida CquotC314 I Ln oP0339 n JvT if Ii1i39 ii iiquot t t1 5h 1 i 3 gtf Q H b Ri393IICO RCHQNII2 CO2 NH You do not need to show the mechanism for trahsinuination 24 Indicate how you would prepare ValAlaLen 391quotou39do not have access to an automated solidphase peptide synlhe izer C 3 I r 5quot 393go o 0CCC2 3 4 144 fgaloo y c gco c r 4 94tr C ca M 393 3 P Ccf gt3C c AJHC LuC0quot C G ass 395 539 lmc44 o 2 9 3 3 CCb0 c fJCHc MH 39 H 20 62 139 C45 195539 3 l g c4czm 1 0 0 39 ce w 5 g I 2 cm 39 W3 45 5 9 5 5 as as VL B gxag L J3 Cg C02 25 H Problem Solving 1 Aliiehexoscs A and B forni the same osazone A is oxidized by nitric acid to an optically active aldaric an d and B is oxidized to an optically inactive aidaric acid Ruff degradation shortens an aidose chain by removing the iii carbon hexoses are converted to pentuses pentcses are converted to tctroses Rt ff degradation of either A or B forms aidopentose C which is oxidized by nitric acid to an optically ac ive aldaric acid Ruff degradation of C forms D which is oxidized by nitric acid to an optically as we aidaric acid Ruff degradation of 1 forms Dgiyceraidehydc Identify A B C and D C C4i39cgt Im A tie ti 39 no I1 H39o i39 14 Ho 14 G H on 4 03439 A store of amino acids that do not separate sufficiently using a single technique often can be so arated by two ditnensiona1 chromatography In this technique a mixture of atnitio acids is applied to piece of filter paper and separated by chromatographic techniques The paper is rotated 90 and th amino acids are further separated by electrophoresis The chrcrnatogram obtained in this way is ca ed a ngerprint The foilowing fingerprint was obtained from a mixture of Arg Asp lie Scr Thr Identify the spots in the fingerprint G Odes gielcitrlotpigoresis r O quotTixv 02 i Otiisf 6 chromatographg The following fingcrpriht was cbtain ad from a mixturis ofSer Asp Len Lys Phe Tyr Identify the spots in the Igampl p1 i1f W 0 L15 electroplxoresis at pH 5 3 O C C O C Text F19 Le ASP Mquot 4 P chromatography ampw 4 F M Q 39 Ala X W OLt3 39 Asp 3 A64 V Lew W Lys 1 6 z cggrgagoresns 4 O O 7 0 SM lLg Val 035 Q I chruxnatography W 5 Glu 055quot V His L 39 E9 fGa9 LN 149 eEltI139o ofess 03w 0 O Met 39 L L Ser J Th 6339 H I ctlarcfajtlafgigraphyyb A nonapoptido undergoes partial hydrolysis to give peptides whose amino acid compositions are shown Reaction of the intact nonapsptido with Edmarfs reagent roloosos PTHLeo What is the sequanos of tho nonapeptido a Elly Ala L o MstAlaIeu a HisVal g MaiLeu 13 GlyGlu d ProSar E GiuProGly 11 Glu Set Val Pro Z a Gig c3 amp 1 t o 2 2 MQ 42 A polypsptizlo can also ho liortially i1ilrolyad ushig t1 Ii fJJ 1ili Eil5 EI Hr otj ciglapiiislaso is 1i3itquotIi35 illE ihat calolyixs iii l1gdrol3 sis ofa poplicio ijontl that is no a ihoa39nti of ii pcpikiocitain l 3psin ci1 39I1csrypsin and olosiaso aro nciopoptidasos glam oaiialyao 1lli1yilml lS of only tho speoifio pmaids bomls lisiad in Table 234 39I r psiofoI ssaiiiplo oainlyzts tho liyclzoiysis oi lino papiiiio bond on ilia Cusiclo of axginiiia or ly ia Cu iiia of iyiirio E 3 E i E aaiigisiif Nil39Til 39Nil lll39f saigzfiif 39 lillil1 an at R iiiis R R quotii quotWquot H H g g H3 arginii1o1r39im ll iiglii Cs sicle of algiailno E I liraiajo fa quot1 I D remains the amino acid sequence of the polypeptide from the following results A id Hydrolysis Ala Arg Gly 2 Lys Mot Pho Pro 2 Ser 39l yr Val C iboxypoptidaso A releases Ala T iatmont vqitli Eltlman s reagent gives PTHVal atmaat with cyanogen bromide yields the folIowiag cleaves on tho Cside of Mot 1 Ala 2 Lys Pho Pro Sor Tyr 2 Arg Gly Mot Sor Val 39Iquot raatmont with trypsin yields the following cleaves on tho Cside of Arg and Lys 1 Gly Lys Mot Tyr 2 Ala Lys Pha Pro Se 3 Arg r Va Tr atmant with ohyrnotrypsin yields the following cleaves on the Cside of Pho Trp Tyr 1 2 Lys Pho Pro 2 Arg Gly Moi Sor391 yr Val 3 Ala Sor maaamoas s The failowing fingerprihi was ubiai i had fronl 3 mixture ofSer Asp Lem Lyra Pine Tyr Identify the spots In the ngerprsnlt V quotquotquot 0 Lisa I electrophorcsis at pH 5 3 O C 1 O u4 4 chromatography 39 H91 ed a W quotgig A O OLt39 Asp 3 J5 A124 M 1 ca 2 ressI o w 0 o 0 51 Vvgd Va 035 Q I cllroxnatngraphy aw Glu O15 His E35 HM Law Len ggegtliogigufeszs 0 O 0 Met 7 Ser 3 Thr 6 M 03 W chromatography La P5 ya umqnuum A oonapeptide ttndergces partial hydrolysis to give peptides whose amino acid compositions are shown Reaction of the intact nonapeptide with Eamon reagent releases PTiLen What is the sequence of the ncnapeptide I a GlyA1a L c Met Ala Lee e HisVal g MetLeu b Gly Glu 3 Pro set E GluProCly hGluSer Val Pro 0 Aquot quot 391 Lquotquot dquot 639 g quotquot3939e39 vquotquotFit 39quotquot541 4 z ME 44 2 A poiygteptitIe can also be lsarttatly E1yt roI39eti using ettdopeptidases At etj tzp E39p l 5 e is an eozyrt391e that eataiyeee the ttydroiysis of e peptide bonti that ianol e theeini of a peptitle citain 391ypsitt CII7In tp3t1 and cigoaase aE l39td0p 1tifElteS tho ezttalyze the tsyttmtyeie of only the specific pepttcie etitzds Hated In Tame 334T393 iItfut e39xai1pTe oataI3zes the itytlrot tia of the peptiite bond on the 3side of arginine of lysine t stoe39ofatgt1tne7 o t L L 39 3 ft at 3 E zxt f t No14 wttrftt gearcacti 39 t tIEt39I E 39 SH ttquot a H R 39 It axquot e to gag y he F it ergintouei a 32 131 3 I L D termine the amino acid sequence of the polypeptide from the following results A id Hydrolysis Ala Arg Gly 2 Lye Met Phe Pro 2 Ser Tye Vat C tboxypeptidaso A releases Ala T Eatment with Ed1 I 13I1 S reagent gives PTHrVa1 I Tr ttatmeat with cyanogen bromide yields the fclletfeing cleaves on the Cside of Met 1 Ala 21 Lye Phe Pro Ser Tyr 2 Arg G13Met S61 Val u 4 Treatment with trypsin yields the following cleaves on the C side of Arg and Lys 1 Gly Lye Met Tyr 2 Ala Lye Phe Pro Set 3 Avg 1 Val Treatment with chymotrypsin yields the following cleaves on the Cside of Phe T1p Tye 1 2 Lye Phe Pro 2 Mg G1yMet Son Tyr Val 3 A1aSer aaeeewea etefeeae Detetmitte the amine seid sequence er a polypeptide from the feliowing results p Ao l V33 Ala Afg I39Ii3i 2 L313 L6 2Mat PTO 2 0 Tlhi in Carboxypeptidsse A releases Vs Bdmert39s reagent releases PTHLee Cleavage with eyanegen bromide gives 3 peptides with the feilewirw amine seid eompositie Cyanogen bromide cleaves en the Cside of methionine 1 His Lye Met Pm Set 2 The Va 3 A1i1gt4 tTi L611 Lye Met Set T1 P3iI1Cat 1 zed hydrolysis gives 3 peptides and 9 steals amine acid frrypsin sleeves en the C side of ergintne and lysine D 1 mg Leu Ser 2 Met Pro 361 Tim Va 3 Ala His Lye Met I 4 Lye a lt ltgea seAsfse see ea sizsss n anIn139 quot wwIuh11 QI1 11 Determine the primary structure of the oetepepticie 39 Acid hydrolysis gives 2 Arg Lee Lye Met Phe 361 Tyr Cerbexytneptidase A releases Set Edman s reagent releases Len Cyanogen bromide forms two peptides cleaves on the C side of methionine I Arg Phe Ser 2 Avg Leu Lye Met Tyr 39l39rypsin forms we peptides and two amino eeids sleeves on the Cside of arginine and lysine 1 Avg 2 Set 3 ArgMet Phe 4 LeuLysTyr gesggegg Determine the primary structure of an eetapeptide from the following data Acid hydrelyeis gives 2 Arg Gly Lye Met Phe Sex Val Carbexypeptidase A reieases Giy Edmelfs reagent releases Val Cyanogen bromide forms we peptides sleeves en the Cside of Met 1 Arg Gly Phe L 2 Arg Lys Met Ser Val Trypsin forms two peptides and two emine acids Cleaves on the Cside ef Arg and Lys 1 Arg 2 Gly 3 mg Met Phe 4 Lye Seat Va eae 3rI 39 Z v 3r 11 a Per each of the following pairs circle the one that weuld form an enhydride more fapidly or CEHOQBJ 12 0 l Of the following sugars which will be oxidized to an optically inactive aldaric acid I4 15 Below are given tha amino acid sequences of three different segments of a protein One exists in another in 1 plaated shear and the third is a random coil Identify which is which aw aa a4 a IiuProThrThrLeuIIuvlluProThrValVaI 14 nxlwm c b GlyAIa GIySerGIya lyAIa Ser Gly TuatLAa S u1quot c LysMetGuSerLeuAlaAsp SetArgMet cs P W K 39 How could you use Uwvis spectroscopy to distinguish between the compounds in each okft 2 following pa139rs at Ci13C01IfCI 39CHCII3 and CII3CHquot 5CH39 CH339CH393 CH 724 7mc M2 5 s 3 V and 7 3 65562772 Lze4l sra6ealt aJ I c CH2mCHCHquot4CHCH quot CH3 and CH3 CHCH39CHCCH3 39 4L 539quot 397quot rquot 9 AT P I v quot1 W W 01Z 39339r in C9 w1 av v 0 lt95gf3 u WA and 0 H OCH e and a 4 vcaa 39 5 39391 393939 zf z39If 39 39quot 7 I7 av a ir 6 j bLysoyme hydroiyzes ccii walls between NAM and NAG residues If H D18 were used in the hydroiysis reaction which ring would contain the radioactive iabei 139 NAG O 0 AM NAG 18 39 h 1 a solution of pH 61 which amino acid would be closer to the positively charged pole me ionine pKa39s 2 E3 and 928 or valine pKa s 2 229 and 974 213 2amp1 61 29 quoti39j 3 12 39 57705 19 44 S 7Ii1illlliCS 32 oints z Answer it foilowing Ha Show the sneci c acid catalvzed reaction if an aldehvde with an alcohol to form a hemiaceiai 20 7 7 6 minutes 10 pints Answer the following a Draw a piI rate profile for ane11211ze thai Iiad we catalytic group at the active site with a pKa 45 that functions as a gcncarai acid catalyst Label both axes i quot Draw the type of graph you would expect to obiain if you were trying to delenninethe rate of iha following reaction Label both axes ciearly i Ho ii 39 CH3 O N0 4 H30 D39 CHC0 0 N01 lg n 450 nm Aa rquotquot39 21 quot 5HunM 22 b which of the following compooiids would react with hydroxide ion more rapidly CH3CH3CH2CH3CH3Ct at CH3CH2SCH2CH2Ci 23 The rats of a chemical reaction is equal to the number of effective collisions in a given volume in a gveo period of time which is equal to rats ofachcmical reaction m gw x B x L What are A B and C A number of collisions per innit time B fraction of the collisions with sufficient energy C fraction of collisions with proper orientatioit 24 39 Of the following parameters circle the ones that wouitl be different for a reaction carried out in thc prcscocc of a catalyst compared with the some rcaction carricd out in the absence of a 39 catalyst sea AH Km Z DQ 25 9 n 53 LeDr2 x 3ior t segn1 ne f 115 peaI Eihfe e bteiif11 Ei 13I i l39tifl 39f iI 5iiig39 L e CH2 QCH2CH3 0 e i gt e 0 1 fi391iiEtI139 1 is 39cie Wljaf Ii1t2139en i are i1 eed ettiii g 0 P 26 I I I L 39im1ee 39e 5i QiquotI I eiep ef the I e 3iEi f the zzgaiki F 21 3ie39 2 5 i39339 1E39 i quot i11 it1 239i3 4 swat tiees it it Ext eei1lze 1ez39e tei en e M L e fl I 0 e M 2 a eeee i 39quot p 53 dwgggg 39i 39 i 139V 33Ifrf 3 inquot1L Ear Z5 l 3 5 g ES i Q g 3 0y G r HQ es vquot1L quot quot 39 27 These are the products of ozonolysis what did they come from O 3 3 3 3 1 G m 1 1 mgctkif V E 393939 F g M g1 e5 ieg3 43 Q a 3e P 23 a Show the speci c acid catalyzed reaction of an aldehyde with an alcohol to form a protonatecl hemiacetai v r 1 O 4 I H53 g 014 I 1 C3 Q b Show the general acid catalyzed reaction of an aldehyde with an alcohol to form a prctonated hcmiaceta Al 8 0 quot39 on If quot39 I K 4 quot IQ Cquotquotquot H I In OOH2 Cid 4 95 6 quotvargt crv A 0 L 0 O 1 59 9 CH3 6 C0 4 bgcy quot I I JG 0350 45 CDC 0 5 J cquot 3quotgtquotquot u v C091 3 C 39 J I7 H I 39 xx 9 0CquotC1 eO Cy 0z gg g4 a 45 S4 9 Os0e4c5co 9 9 OC 3 0 C 0 0 0 J 3 NI 1 I 5530 062 KC 4 W c I 3939 0 A M av er en 5 2 W v A quot Q quotquot 05 fba i 5 A0 I K 9 Sfgk zf 9 H 39 CCJ av C559 6 quot06 H 39 cc Q0 p1 37 g 67 Lt3 CE I UH 1 11 391 Gquotquot 9 fE F Q Ct 39 M gt1 39 39 5quot LHi Qx CxS 339 gu3g R E 5 H 4 a HB Cu3 ur 13 3 xx LC Q137 r1 5 O H 33 9 p quot 39 I Q C DP5 cu 2IH 39 N C M PTP L 11 393 gt if L0 quot 3 J 3 Lt u L 39quot L 3 D Pd u M 09 e 539 lIcj39 5 Lg o EX NII1iHHgo gt f H h1E 5O If H 5 M 1 is gt L0 gt INHL 33 quota oH 41f o H 393quot H hr 1 cucc a 9 quot 3quot H ucoa E1 8 I 2 gt HC h39CquotU Li11ooo ltlLltn 1 D I H L e mmE mHgt N 14 U1 L93 39 Dgl39IJLI H g03939 H H D 97 p 0 t eca a ME yuuodi L 7 7 r a A 0 9 Q C Q5 oH 3 5 H a C I 9 H Ho 0 K quot 3are to F 39 SJ 1 cgt 5 quot 5 f7 DH Fquot 54 Cit 3 TC 5 B 7 X EH2 LEE OH h E l C quotO H H I quot139 0 K 1 E a a quot5 F1 J3939 S Cu in Q gt39 quot 4 p hfDXS Zzquot 17 5971E cry3 c 7wcggt7quotquotquoty J3 0ClJ7kJC 74 X 1r 9Lquot2 Z3 JH7 5 92 9 quot07ln N ar 909 X quot3 J xv 73fawaA x7 1F tjlr 9A I4 g40lt JMM 5 J E L 05 03 39 0 Jr C r39r39 C 9 3 J kg m 0 C go quot C 2 Llt lt3 Z 9 Uf mh Ab re 006 miuhe 2 Conquot27 sor Mn C 1a a 3 cf Nr N F l K Qhd 5L9 Q A1107 1Az j 54 u1 mag J 725 6 4 715 7777 7L 7392 5 ye Auund 72 auao rmr r3971r 7 1 c22 no 39 g mac 9 246 Q3 5390 K yj 512ltj W3 C a Zz 0 J 7 0 quotlt37 quotJ 45 39 757 quot r quotquotquot 7quot7 7 rc7539or cu igooaE1 0rzaa uo F913 39 02m5 39 N419 amid dd33 516C n C4ocaji j KC 7392 F40 O I quot9CX3 9r FC a 9 C45 9 W WA 6 4 25061 lt34J5 CK9 C142 Ix fCal 9 0 C G73 az3 C amp f Cg Cjod39 C0d 1 fr7H 0j lt1 040 cs999 1foltgtj Q0 E 93quotquot 99 39539 39 33oo curt Answere to Claapte139 13 Practice Test 0 9 koc1391 1050 or 1250 cur O JNH2 f CI 13131 IQCEI 3 CHCH3 I 1500 our 3 I00 curl g e gcezea CH 3300 em391 A21 mo cur H CH3CHQC E CCH3 21oo curl CH3CH2CIIQCHZOH 35oo 32oo curl cgcg13 1383 cur OH The H stretch of a concentrated solution of an aicoltoi occurs at a higher t reqnenc3r than the 0nH stretch of a dilute solution Light of 2 pm is of higher energy than light of nm It takes more energy for a bending vibratiott than for a stretelling vibration Propyne will not have an absorption band at 3100 em 1 because there is no changei11 the dipole moment Light of 8 out has the some energy as Eight of 1250 cor The M I 2 peak of an alkyl chloride is half the height of the M peak A ehromophorc that exhibits both 22 a at and or gt 5 trtmsitions will have the n gt z transition at it longer wavelength CH3 E CH3CHgl3CiI2C39IgClI3 OH Absorbanee 110111 absorbtivit539 K concentration x length of light path in cm 0772 molar absorbtivity x 38 x 10 x I inoia139absorbtivlty 1900 M4 curl H joH E0H 1 tIt 3100emquot 2GUcmquot1 15Gt cor 9tD cor 1330 cm quot quot139lquot3 T1 quotI quot11 Atlswcrs O O 9 OH 00113 9 I 33U0 2500 cmquot 290U cmquot G100 cm 2900 our 39138cm a1330 cur i050 C111quot 0 l Q 170O cmquotI rI050 cu H E l bi Na 3 NR2 Ahsmrhance molar tbso139btivity gt1 conccntmtion gtlt length ofEigl1t path in cm 076 1200 X cuzlcei ration c011cc11iraiion 63 gt 10 M 1 mm era to Cim Jter ijm 0 0 ll 9 V 39 V 41 H3CHgCH3 CH3 CH3CHgCHCH2H3 CH2LH H 394 3 1 4 39 CI 39 EH3 33 N03 u CH3CHCH2CHCH3 3 3 3 II 0 O n I CH3CH3CCH3 H N03 CH3CH2COCHgCH3 quot quot3939 ll3939p6l Fm tri C L H H I CH3 1 dolihl t fI WC dcmblat nn iiplet doublets Cm H Cl CH3OCHgC HgCH30CH3 BrCHgCH2Bi39 I I 1 quintet singlet O O 0 l l l 39 CH3 OCH 2C H 3 Cil3CH2 OCH3 H OCH3CI igCI39I3 3 signals 3 signals 4 signals The signal at the laigliesi The signs at the highest 39 frequency fs licst frequency fsrllmst downfisid is 1 quarter dowil slri is it singlet The peaks on the right if an NMR sjiccitmlrzl are desiiieidecl coiilpstsd 10 the peaks on the left n I Dimctllyl ketcms has the same numbs139 of signals in its H NMR speclnun as in its 3930 NMR spectrum c In the H NMR spsctmm of the counpound shown below H16 lofr eslf139cque11cy signal the one farthest upfielcl is a singlet and the highest frequency signalthe one farlliest downfield is a doublet 1 Tile greater the ft squenc39r of the sigma the greangzr its chemical shift in quotppm t 39 septel H CH3CHgCH2Ci I CH3CHgCOCH3 1 CH3CHCH3 iriplel singlet liar 3 signals 3 signals 2 signals ll 1 Cii3CHgCH2Cl I3 CH3CHgCOCH3 C CH3CHCiI3 3 signals 4 signals 1 triplet singlet I 2 Signals doublet 8 ampnve139s to CI1apte139 20 Practice Test mdtlction 39 0 II C CH3CHpCHi 0II no reaction CH3CH2CH2NHCHgCH3 390 H 00 1 0i1 IiIJl1 C I II CH H g It 0 II CH3CH2CHgCH OH CH20H CH3CI IgOH EH CH3CHgCH3CHCHgCH3 CH3 1 CH3CH3CHgC 39 O 4 CH3 CHZCOH 397 3 05 39s9 39 A320 NIL 4 II32 CF13 H3C I130 C C and CH3CHg CHZCHS CH3C Ig NaBH4 is fl weaker xjeducing agent than LiAlH4 Esters am easier to reduce man ketones In an oxiciatiomrcdttcliun reaclion the oxidizing agent is oxidized Ketoues are reduced to primary alcohols Aldehyde3 are oxidized to carboxylio acids Acyl halides are oxidized to aldehydcs Alkenes cannot be reduced with NaBH4 OH CH CH 2 3 CC CH3 5 H0quot II CH3CHCHgCH3 i CH3CILIgIIC113 ma CH3CHgCHCH3 33i99i CH3CH2CCH3 B B1 103 2ZnH2O or 103 2C3H32S quot39J393 TJquotId39Eir3 3 NHnae uenyltelralxydmfcfaie transfcm a ftrsixyi gzwp is the subsmass I Pquot A cataiyst mas neat affesci the eqa ibrium canstan of a mansion F c I132 11 at iyslysuiys is gr a1ar than any Cafifs imii idual quotgrim waives pC F d The 91 of i 1r3r1 is 45 I Cymsiuaa f niai1139 as pu tw ring 0 F Iiioiin is 2 cizfaelar fer decartgt r39Iatiran rma39s i 9112 T g Lipoic acid is ctwahntly bcgzind is its cimyms by an imines iiakags T v 3911 C u3n1pIexing with a xnetal ion insreaam tbs gm g 9 Wm nmkes it have 3 larger vaiu g T L E113 metal atom in vitamin B12 is 33932quotquot T J 331 pfa at a mrbaxyiie 3355 i 2 greater in a nanoiar sehez that it is in 2 99 sum LD 39 F k T113 equilibrium ccmsiant af a mactzican whasc pmaducts 3239 mm ab t F I re grants is greater than I 1 In papa ciwolnatogmplay wmsine 39A39s39ltr1IaI axiom f1uti1lt r up the paps392t 3L 391tt wazmid pwnylzianIn T 339 2 I fErythriise 59311 aidairiase 1 gr 5 1 Naturally meaning 1onew c1s1ridcsh nv 112 Lcan gaxrathan 3 Mo1GsaCcI1arid s that form 5 mcmbltrc i rings are tuned furancrses fl C rboxgrgegnticlhse A is an eneciopeptidasc g A mini is reduced to 3 iisuIfidr Indicate whether each or the t alluwing mactions is mm at mm a A caa yst increases the equilibrium co stasxt cf 2 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