Please answer all parts of the question in detail, thanks The following molecule was once considered as a drug candidate by a large pharmaceuticalcompanya.HOFor the functional group indicated, write the pKa expression for the group acting as anacid and identify an appropriate pKa value using the table provided.b. For the functional group indicated, write the pKa expression for the group acting as abase and identify an appropriate pKa value using the table provided.c. Use your pKa data to predict whether the group will act as an acid, base or both whenused as a drug.d. Use your pKa data, and answer in part c, to predict whether the molecule is likely to besoluble at pH 7.4. HProtonated NitrogenNH4+EtNH3H₂N.IPr₂NH₂*PhNH3*PhN(Me)₂H*Ph2NH2H₂NNH3*Et3NH*PhHN4.9NN=NHeterocycles23.3HNܒܘ15.120.9N-NN29.414.6NH₂HNNH₂HAmidesHPh9.210.610.754.65.20.788.1211.18.3618.6H-N0₂16.122N-N25.221.3NH₂Selected pKa ValuesAminesHN3NH3iPr₂NHTMS₂NHPhNH2ΝΗHNX = CH3Carboxylic acidsOHCH₂NO2CH₂FCH₂CICh₂Br6.04.73836263144CC13CF 3HC6H5CH3CHCHΘΗ -2.5HNⒸH 3.24.761.682.662.862.860.65-0.253.77ProtonatedHeterocycles4.23.0NH5.25HN-NHN-3.67.1PhPhImidesNHNHPhФонPh OHФонOHMeProtonated SpeciesⒸOHCH3HHHOHMeOHiPrOH8.30AlcoholstBuOHС6H5OH14.70PO₂NC6H4OHPOMeC6H4OH-12.4-7.8-6.2-3.1-2.05-2.215.715.516.517.09.957.110.2

Acids are species with the ability to donate a proton and bases are species with the ability to…

Answered: The following molecule was once…

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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Similar questions

A simple biochemical reaction with three molecules has solutions that oscillate toward a steady state when positive constants a and b are below the curve b - a = (b + a)3. Find the largest possible value of a for which the reaction has solutions that oscillate toward a steady state. (Hint: Find where da/db = 0. Derive values for a + b and a - b, and then solve the equations in two unknowns.) Source: Mathematical Biology.
For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in both reactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitive or uncompetitive. ( see attached picture ) how I and S bind to the E as shown by the Lineweaver Burk plot. the significance of the following obtained values for Km and Vmax. effect in slope and x-intercept
You are investigating inhibitors of chymotrypsin, and the two molecules shown on the right (A&B) are being considered. Draw a Lineweaver-Burke plot showing the expected effect of each of these molecules on normal chymotrypsin kinetics. Indicate which molecule you would pick as the better inhibitor. You want to improve the inhibitor you selected above. Briefly describe one key change you could make to your molecule to make it a better inhibitor. Justify your answer.
Drug X has the following properties: Multiple H bond donors and acceptors, a low log P, a low solubility in octan-1-ol, low molecular weight and contains both amino and carboxylic acid functional groups. Which of the following statements about the predicted oral bioavailability is TRUE? A. The drug will likely utilise the passive transcellular pathway. B. The drug will probably display increased oral bioavailability when taken after a high fat meal C. The drug resembles an amino acid and could be absorbed by the folate transporter D. The low logP suggests extensive partitioning into the phospholipid bilayer of the small intestinal mucosa E. The drug could be absorbed by the amino acid transporters expressed in the small intestine
a. Calculate both Vmax and KM for the control using Lineweaver-Burk curve. b. Provide the type of inhibition for both? Find, KI, for the inhibitor binding to the enzyme, for experiments (2) and (3). d. Calculate the reaction Kcat for the Control in experiment (1). e. Draw a velocity versus [S] showing Michaelis-Menten curve for the Control. Clearly show Vmax and Ky for the enzyme. c. (1) V. [(umol/(ml.s)] 7.6 (2) V- Τ (μmol/ (ml.s)] [S] (mM) (3) V. [(umol/(ml.s)] 6.6 2 4 14.6 26.6 45.8 4.4 8.6 16.4 29.8 11.4 17.8 24.6 28.2 16 24 60 40.8
Give an example of a noncompetitive inhibitor and its target enzyme. Draw a hypothetical Michaelis-Menten curves in the presence and absence of the noncompetitive inhibitor. Discuss the effects of noncompetitive inhibition and the reasons for these effects on the values of Km and Vmax.
Which physicochemical properties are useful for prediction of the oral bioavailability of drug molecules? Use naproxen and propranolol as examples in your answer.
Which of these heterocyclic drugs is likely to be the least soluble in water? Use the Fsp³ parameter to decide. OH Tramadol Chemical Formula: C16H25NO2 YOUR OW Pantoprazole Torasemide Chemical Formula: C16H15F2N3O4S Chemical Formula: C16H20N4O3S Temazepam -OH Chemical Formula: C16H13CIN₂O2 Tioconazole Chemical Formula: C16H13C3N₂OS A. Tramadol B. Pantoprazole C. Torasemide D. Temazepam E. Toconazole
Shown below is a proposed mechanism for the cleavage of sialic acid by the viral enzyme neuraminidase. The kcat for the wild-type enzyme at pH =6.15, 37 °C is 26.8 s-1.(a) Describe the roles of the following amino acids in the catalytic mechanism: Glu117, Tyr409, and Asp149. List all of the following that apply:general acid/base catalysis (GABC), covalent catalysis, electrostaticstabilization of transition state.(b) Based on the information shown in the scheme, would you expect mutation of Glu 117 to Ala to have a greater effect on KM or kcat?(c) For the R374N mutant at pH = 6.15, 37 °C, kcat is 0.020 s-1, and KMis relatively unaffected. Based on this result, it seems that R374 is morecritical for catalysis than for substrate binding. Explain how R374 stabilizesthe reaction transition state more than the substrate (i.e., what feature of this reaction would explain tighter binding to the transition state vs. substrate?).
Given the following choices,a. what is the structure of the product of the reaction catalysed by ACAT?b. structure of the product produced from the reaction catalysed by phospolipase A2?c. general structure of TAGd. structure of glycerol
HOW TO SOLVE THIS IN EXCEL? For the following aspartate reaction in the presence of inhibitor, Km = 0.00065 M. Determine Vmax in both reactions and in the reaction without inhibitor, the Km. Identify whether the inhibition is competitive, non-competitive or uncompetitive. ( see attached picture ) Briefly explain: how I and S bind to the E as shown by the Lineweaver Burk plot. the significance of the following obtained values for Km and Vmax. effect in slope and x-intercept
Describe reaction between AP and PNPP and how is used to determine the kinetic parameters of AP. i. İndicate the value for the activity of AP(which is 3.08) What does it mean? Is your enzyme active or not? What does it say about the purity of your enzyme? ii. How the purification process affects the activity?

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