Problem 1Nelfinavir is a small-molecule treatment for HIV that acts by inhibiting HIV protease, a critical enzyme forviral replication.OH 2CHO.OH 3Nelfinavir"BUHN(a) The pk, of the protonated form tertiary amine (1) in nelfinavir is 6.00. In general, the pKs ofprotonated amines (i.e., ammonium ions) range between 9 and 11. How would you rationalize thisapparent discrepancy?(b) The pK,s of the two -OH groups (2 and 3) are 11.06 and "17, respectively. Briefly explain why thepK, of alcohol 2 is 6 orders of magnitude lower than that of alcohol 3.(c) Draw the form (i.e., protonation state) of nelfinavir that you expect to predominate in the stomach,where the pH is between 1.5 and 3.5? Briefly justify your answer.(d) The pH of saliva is about 6.5. What two forms of nelfinavir would you expect to predominate insaliva? What are their relative ratios?

"Since you have asked multiple questions, we will solve the first two questions for you. If you want…

Answered: Problem 1 Nelfinavir is a…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Questions 11-13- refer to the carbohydrate mannose (open chain and one anomeric ring configuration of the structure shown below) HO HO H H CHO H H OH OH CH₂OH OH H OH f HO HO- H H OH H 11. Draw the open-chain structure of mannose following oxidation of the carbohydrate to an aldonic acid 12. Draw the open-chain structure of mannose following oxidation of the carbohydrate to an aldaric acid using NO3 13. Draw the structure of mannitol
QUESTION 31 Four competitive inhibitors of an enzyme were found to exhibit the following K¡ values. Which is the worst inhibitor? K = 7x 10-5 M K1 = 3 x 10-6 M KI = 1 x 10-4 M K1 = 6 x 10-8 M QUESTION 32 What is the Km for a Michaelis enzyme if the 1/concentration of substrate intercept is -5.73e Mon a Lineweaver Burk plot of its reaction kinetics? Give your answer in 3 sigfīgs in scientific notation, for example, 1.52 e QUESTION 33 What is the charge of an ionized peptide in the mass spectrometer if its isotopic peaks are 0.20 m/z apart? O 6+ O 5+ wers to save all answers. stly cloud
Problem 3. Describe (in words or by illustration) the overall subunit composition of the protein complex supported by the experimental data below. Indicate the presence of covalent interactions (such as disulfide bonds) and/or non-covalent interactions (electrostatic or hydrophobic interactions) involved in the complex Molecular mass by gel filtration: 200 kR Molecular mass by SDS-PAGE without DTT: 40 kR and 120 R Molecular mass by SDS-PAGE with DTT: 40 kD and 60 kD
CIA Problem 20.1 Look at the structuros of the blood group doterminants. Red blood cell N-Acetyl- D-glucosamine Blood D-Galactose L-Fucose type O Red bleod cell N-Acotyl- D-glucosamine Blood D-Galactose L-Fucose type A N-Acetyl D-galactosamine Red blood cell Blood N-Acetyl- D-glucosamine D-Galactose L-Fucose type B D-Galactose Part A Choose the right statements about human blood types. [Cell-Surface Carbohydrates and Blocd Type, p. 672 in the textbook] Check all that apply. Blood group A has a moleculo of N-acetyl-D-glucosamine linked to D-galactose. Blood group O has N-acetyl-D-glucosamine linked to D-galactose and D-galactose linked to D-galactose. Blood group B has D-galactose linked to D galactose. Blood group A has D-galactose linked to D-galactose. Blood group AB is thə univorsal donor because it has components common to all blood groups. Blood group O is the universal donor because it has components common to all blood groups. Blood group B has a molecula of…
8
Processing of results Calculate (and show your calculations) for each acetic acid solution 1. the molar conductivity, Am (S m² mol¹), 2 the degree of ionisation, a 3. the ionisation constant, Ka 4. [H3O] = αcм and the pH = -log [H3O+]. Finally, calculate an average value for the ionisation konstant, Ka, of acetic acid with its standard deviation. Compare your result with a literature value and make a statement whether it is significantly different or not.
15-80 what is the chemical formula of the inorganic product formed, if any, in each of the reaction in Problem 15-78
PROBLEM 2: A biochemist dliscovers and purifies a new enzyme, generating a purification table below The step of protein purification Total Total Specific Total The multi- Total activity yicld (%) cnzyme fold protcin (mg) maltifold activity increase in purification (units) purity Whole-cell lysate 8.4 LO 500 l00 4200 40% ammonium 22.2 95 2.64 9.64 180 3990 sulfate Ion exchange 90.2 251 6.63 68 3787 55.7 Gel filtration 50 5000 to0 119 1.8 11.9 (a) From the information given in the table, calculate the specific activity of the enzyme, total yield (%), multi-fold increase in purity, and total multifold purification after each purification procedure. b) Which of the purification procedures used for the enzyme is most effective (Le., gives the greatest relative increase in purity)? (c) Which step - ion-exchange or gel filtration chromatography - causes the greatest loss of the protein. (d) If you wanted to use only one purification step, which technique would you choose?

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