3. Assuming the presence of acids HA and bases (A) as needed, give a plausīble mechanism (think Markovnikov addition and Zaitsev rule) for the isomerization of isopentenyl diphosphate (IPP) into dimethylallyl diphosphate (DMAP). IPP DMAP isomerase OPP isopentenyni diphosphate OPP) dimethylally diphosphate (DMAP)
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- Which group of side chains is most likely to take part in the catalysis during an enzymatic reaction? Substantiate the answer.PLEASE TURN ΤΟ ΤHΕ ΝEXT PAGE 1. (a) Describe the steps that occur when a polymer is dissolved. (b) Do you expect solubility parameter (8) values to increase or decrease as the molecular weight increases in a homologous series of aliphatic polar solvents? Explain your answer.discussion of the "Green Chemistry" aspects of the Thiamine catalyzd reaction, and the pros and cons of the cyanide and thiamine catalyzed reactions.
- d) 7-hydroxycoumarin forms one-dimensional hydrogen-bonded chains in the solid state. Coumarin-3-carboxylic acid forms hydrogen-bonded dimers. Coumarin does not show hydrogen bonding. (i) Using a diagram, define the term hydrogen bonding and use your answer to explain the differences in hydrogen bonding between the two molecules. (ii) Draw the hydrogen-bonded chain observed in 7-hydroxycoumarin and provide the graph-set notation to describe the motif. You should show at least 3 molecules. (iii) Draw the hydrogen-bonded dimers observed in coumarin-3-carboxylic acid and provide graph-set notation to describe the motif. You should show 2 molecules.1. To pass Chem 18.1, ELIBAP must be able to determine the melting points of three ester compounds extracted and purified from three different plants. Ester 1 Ester 2 Ester 3 :0: H. MW: 182.17 g/mol MW: 152.15 g/mol MW: 164.20 g/mol Possible Melting Points: -31 °C 64-67 °C -9 °C a. Given the molar mass and molecular structures of the esters, determine their most possible melting points. b. According to her friend who took Chem 18.1 last semester, one of the ester compounds exists as a solid above room temperature (25 °C) while the rest remain in their liquid forms. Identify the ester which is present in solid form above room temperature. Draw the structure.For the base-catalysed hydrolysis of 3-bromo-3-methylhexane (i.e. reaction with the nucleophile OH-): For the reaction intermediate, draw its structure and give the VSEPR description of the geometry at the reaction centre Give the names and draw the structures of the two reaction products. Explain your conclusions.
- When oxalic acid is added to water the oxalic acid will dissolve. If D2O were used in place of H2O would the deuterium become incorporated into every site where there was a hydrogen atom in the original structure? Explain2. Explain the following: (a) How sites of variable activity in a heterogeneous catalyst might result in a polymer of high polydispersity. (b) Why molecular hydrogen is useful for controlling molecular weight in Ziegler-Natta polymerization. (c) Why only coordination catalysts are effective for polymerizing propylene and higher 1-alkenes.How do u account for the observed solubility of C10H8 and urea in H2O based on the nature of the bonds that exist in them?
- Explain how the light naphtha isomerization catalyst is bifunctional.What is the location in the catalyst of the different kinds of sites and what function do they serve?9. Phosphotyrosine (shown below) has four ionizable functional groups (pK1 = 2.5, pKR1 = 2.1, pKr2 = 7.2, pK2 = 9.5). (a) Write the equilibrium equation for its four ionization forms and assign the proper pka for each ionization. DRAW the structure of phosphotyrosine in each ionization state. What is the net charge on the phosphotyrosine molecule in each ionization state? *H3N. pk2 - 9.5 .COOH pK, - 2.5 O=P-OH pKRI - 2.1 ÖH pKRI - 7.2 (b) Draw the titration curve of phosphorotyrosine and indicate each pKa and the isoelectric point (pl), indicate the molar equivalents of OH on the x-axis.(a) Describe in detail how you will determine the primary structure of protein. You have been given a mixture of lysine, histidine and cysteine. The isoelectric point of the amino acids are as follows: Histidine 7.64 Lysine 9.74 Cystenie 5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.