2427 (a) The isoelectric point (gD) of phenylalanine is pH S.S. Daw the structure of the major form of phenylalanine at pH values of 1 5.3. and 1 (8) The isoclectie point of histidine is pH7 6. Draw th stuctures ofthe major forms of histidine at pH values of 1 4 1.6, and 11, Explain why the nitrogen in the histidine rng isa weaker base than the amin group. (e) The isoslectc point of glutamic aid is pH 3.2 Draw te structures of tbe major forms of glutamic aid at pH values of 1,32. 7, and 1. Explain why the side-chain carboxylic acid is a weaker acid than the eid group next othe srcarbon ato. 24-28 Draw the complete structure of the following peptide Ser-GieMet- NH5 Predict the products ofthe following reactions. @ » Hs kee OH pytiae Ph—CHy-0—C—NH—CH— coon Es ‘OH ba ° (6) Lys + excess (CH;CO)0 —> (@ (bipnine Meese! e HO Ho, ° Nit, HON ( product fom pute) 8%, cH,cH, cua " 10 (g)4-metlpentanoic acid + BePBr, + (h) product fom pust(g) + excess NH, ——> ‘Show how you would synthesize ay ofthe Mandar amino aids from cach starting material. You may use any necessary eagents @ ° () CH EH—CHe—COOH fe (CHY,CH—CH—CHO (CHysCH— C— COOK cnn, ‘Show how you would convert alanine wo the following derivatives. Show the suucture ofthe product in each case (a) alanine opeopst ete (@) Nebcazostalaine (©) Mbenzylorycabonyl alanine (4) tersbutyoxycasbonyl alanine Ce etn asc eseacis (CH—CHOH—COOH sesiepihtnesisn se ace rar cele acts re elloving pepe Tl whe cach ple ici bas eta (a) methionyltvconine (©) thacoaylmetionine (©) srsinylaspnylysne (@) Ghu-cys-Gin “The following structure i ran in an unconventional mannee es ° ° enjen,—G1 enn en —enyen,—d, doxn, NN co—cHNH, (a) Labo he N terminus and the C teins. (@) Lake he peptide bonds () deuity and label each aminoacid present. (@) Give the ull mame and the abbreviated name, Aspartame (Nurawes®) ca remaahly secon dipeptide exer. Complete hy of spare gies phenyl slonins, spat cd, an man. Mi incabaon with aroypepdse hs mo eet on aspartame Treatment of Ssparae with pay soduocyanafllowed by mad yal gives he pelo of aspar c Prope str fo aspartame A nloclr weight cena hs show tha an unknown pepe a penapeptie, an an ani ac ans ‘tows tat conta he ullowing reduc one Gly vo Ala ete ME one Phe. THeaent he gl pepe ‘th catnypepiane give santa the fs fie amino cd released: Spent west of he peapeide wth Phenyl ohncyant followed hy mild daly ives the flowing deste: mi anion man awn yen Shem ofa Propose a sive or he unknown pentapeptidesf Sow the steps and intermediates inthe synthesis of Leu-Ala-Phe by the salidephase process. Pepiides often have functional groups other than free amino groups tthe N terminas and oer than carboxyl groups athe C terminus, (a) A terapeptideis hydrolyzed by heating with 6 M HCl, and the hydrolysates found w contain Ala, Phe, Val and Glu ‘When te hydrolysates neutralized, the odor of ammonia is detected. Explain where this ammonia might have boon incorporated i the original pepe. (by The tripeptide thyrotrpic hormone releasing factor (TRE) has the fll name pyroghtamythistid proline. The stcture appears Here. Explain the functional groups atthe N terminus and atthe C erin, (©) On adic hydrolysis, an unknown pentapeptide gives glycine, alanine, valine, leucine, and isolenine. No der of| ammonia is detected when the hydrolysate is neutralized. Reaction with phenyl isothineyanae followed by mild hydrolysis gives no phenylthiohydantoin devvative. Incubation with cahonypeptidase as no effect. Explain these findines.Complete hydolysis ofan unknown basic decapepie gives Gy, Ala Leu, le, Phe, Ty, Glu, Arg, Lys, and See. Tesi residue analysis hows thatthe N terminus is Ala andthe C terminus i Te Incubation ofthe decapeptide wit chymotry Sin gives two wipepides, A and B, and a eapepide. C. Amino acid analysis shows that peptide A contains Gly. Glu. Tye, aod Ni; peptide B contains Ala, Phe and Lys and peptide Ccoatans Leu, le, Ser, abd Arg. Temminal reside analysis ives the fllseng eas © Ae Wie Incubation ofthe decapeptie with uypsin gives «dipeptide D, a pentapeptide Band wipeptide F.Tesmina residue sialyl of F shows thatthe N terminus Ser and the € terminus se, Propose a structure forthe desapepide aod for fragments & through “There are many methods fr activating a carboxylic cid in prepaton for coupling with an amine. The fllowing method ‘conver the aid to an hydronysucinimide (NHS) esr. Lie eS ° ne. eon) Ba, - neon ? z NS ester (4) Explain why an NHS exer s much more reactive hana simple alkyl ester. () Propose a mechanism forthe reaction shown. {Propose a mechanism forthe reaction ofthe NHS ester with an ane, R— NTs Sonmctines chemists acd the unnatural D enantiomer of an amino acid, often as pat of «deg oan insecticide. Most "amin acids ar solsed rom peteins, but the pari acids ae ely found in natal prseins. amino acids ean bo ‘yaihesized from the corresponding -amino acids, The following spathctic scheme sone ofthe possible methods. oot coon bog NEOs inomatier MY, incite? Hs uy Nh ws contin contgution (a) Draw the structures of intemites fan 2 inthis scheme, ()) How do we know tat the products eniely the unnatural » configuration? ‘A student wok the proton NMR specu of phenalanine in D;O solution, and had the insrumet suppress the DOH Solvent peak. The spectrum is shown below. The integrated lative aeas of the peaks af 5:11: (@) Draw the structure of phenylalanine as it exists in DO solaton, There ia lage excess of D0, and any exchange= able protons in pheuyllunine wll exchange withthe selveat) () Assign the peaks inthe spectrum tothe protons in the state (©) Why don’t we se the NH or —COOH protons in the spectrum? (@) Whatis the elaonship betnecn the 180 protons that generate nearly mitrorsimage maliplets at. and 3.37 storm