1. Gemtuzumab and Trastuzumab emtansine are two examples of mAb-drug conjugates(ADCS) where the thiol-containing drugs calicheamicin and DM1, respectively, areattached to the mAb's via the linkers shown below.SO, Na„SHThiolhydrazide in GemtuzumabSulfo-SMCC in Trastuzumab emtansine(i)Show the chemistry involved in conjugating the drug (Calicheamicin-SH) to theantibody in Gemtuzumab and draw the target mAb-drug conjugate with a detailedlinker region.Show the chemistry involved in conjugating the drug (DM1-SH) to the antibody inTrastuzumab and draw the target mAb-drug conjugate with a detailed linker(ii)region.

mAb (monoclonal antibody) are antibodies which have monovalent affinity i.e., binding only one…

Answered: Show the chemistry involved in…

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

See similar textbooks

Similar questions

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
2. The two diagrams to the right il- lustrate plots of steady-state ki- netic studies to characterize the in- FB 0.8- nH = 3.5 0.6- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is smaller than that for the natural 0.4- 0.2- 10 μΜ 20 μΜ 48 μΜ substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 2- 3.2- 0.4- concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no AMP (•), 10 µM AMP (•), 20 µM AMP (-), and 48 µM AMP (-). -0.8- 4 12 20 28 36 44 52 60 68 76 84 92 1.2 1.6 2.0 2.4 [AΤP (μΜ) log[ATP] (µM) (a) how ATP interacts with the enzyme in the case of no AMP (•). Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe (b) with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the…
6. The Vmax and KM values for an unusual hexokinase found in Try- pansoma cruzi (the causative agent of Chagas disease) are shown in the presence and absence of a bisphonate inhibitor (structure shown). Without inhibitor With inhibitor Км (mM) 90 125 Vn max (umol min-1. mL-1) 0.30 0.12 ОН O=P-O- A bisphonate compound a. What type of inhibitor is bisphonate? b. The parasite hexokinase, unlike the mammalian enzyme, is not inhibited by glucose-6-phos- phate but is inhibited by pyrophosphate (PP;). Is this observation con- sistent with your answer to part a? c. Might bisphonate be a good candidate for a drug to treat the disease?
Asap
2. The two diagrams to the right il- lustrate plots of steady-state ki- netic studies to characterize the in- teraction of heart muscle phos- phofructokinase-1 with a non-phy- siological, synthetic substrate fruc- tose-6-sulfate. Because the kcat is smaller than that for the natural 5 0.8- NH = 3.5 0.6- 0.4- 0.2- 10 μΜ 20 μΜ 48 µM substrate, higher enzyme concen- trations could be used. The results show the influence of increasing 2 0.2- 0.4- concentrations of ATP on the initial -0.6- > velocity of the enzyme catalyzed reaction in the presence of no -0.8F 4 12 20 28 36 44 52 60 68 76 84 92 .2 2.0 2.4 ΑMP () , 10 μΜ AMP (+ ) 20 μΜ AMP (-), and 48 µM AMP (-). [AΤP] (μΜ) log[ATP] (µM) (a) . Write the reaction in words catalyzed by the enzyme for the alternative substrate, describe how ATP interacts with the enzyme in the case of no AMP (•). (b) ! with respect to the binding of AMP and ATP to the allosteric effector sites on the enzyme. Explain the physical significance of the displacement…
5 25) Although the UV280 extinction coefficient of BSA is well known, why was the BCA assay employed to measure protein concentration of the folate labeled BSA? Please provide an explanation. (C) Would the use of reducing agents have an affect on the tertiary structure of BSA—please explain your answer (you will need to investigate the structure of BSA beyond this article)?
2. Draw the structure of pentapeptide Trp-Asp-Cys-Lys-Gln that would predominate in aqueous solution at pH=5.5. (Relevant pKa values are 2.2, 3.8, 8.3, 9.6 and 10.5.)
3. Solve the sequence of an oligopeptide 7 residues long which gave: Asp Leu Lys Met Phe Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. The PTH derivative from Edman degradation was c. Brief chymotrypsin treatment yielded several products including but not limited to a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and a free Lys.
3. Solve the sequence of an oligopeptide 7 residues long which gave: Asp Leu Lys Met Phe Tyr The following facts were observed: a. Trypsin treatment had no apparent effect b. The PTH derivative from Edman degradation was c. Brief chymotrypsin treatment yielded several products including but not limited to a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lys, and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and a free Lys. Instructions Make use of the table below to determine the sequence of the mystery protein.
Crystal structures exist for three neurokinin-1 (NK1) ligand complexes with the following pdb codes (6hll, 6hlo,6hlp). State which is the highest quality crystal structure indicating the criteria you used to evaluate this.
b) Consider the following experimental results: Total hydrolysis of a nonapeptide gave: Ala,Arg, Glu,Leu,Lys,Met,Phe,Tyr,Val One fragment from CNBR treatment was: Tyr-Leu-Lys One fragment from Chymotrypsin treatment was Arg-Glu-Met-Tyr One fragment from Trypsin treatment was Val-Ala-Phe-Arg i. Deduce, with suitable explanations, the amino acid sequence of the nonapeptide.
At 37 °C, the serine protease subtilisin has kcat = 50 s-1 and KM = 1.4 × 10-4 M. It is proposed that the N155 side chain contributes ahydrogen bond to the oxyanion hole of subtilisin. J. A. Wells and colleagues reported (1986, Phil. Trans. R. Soc. Lond. A 317:415–423) the following kinetic parameters for the N155T mutant of subtilisin: kcat = 0.02 s-1 and KM = 2 × 10-4 M.(a) Subtilisin is used in some laundry detergents to help remove protein-type stains. What unusual kind of stability does this suggest for subtilisin?(b) Subtilisin does have a problem in that it becomes inactivated by oxidation of a methionine close to the active site. Suggest a way to make abetter subtilisin.(c) Is the effect of the N155T mutation what you would expect for a residuethat makes up part of the oxyanion hole? How do the reported values ofkcat and KM support your answer?(d) Assuming that the T155 side chain cannot H-bond to the oxyanion intermediate, by how much (in kJ/mol) does N155 appear to stabilize…

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781319114671

Author:

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

Publisher:

W. H. Freeman

Lehninger Principles of Biochemistry

Biochemistry

ISBN:

9781464126116

Author:

David L. Nelson, Michael M. Cox

Publisher:

W. H. Freeman

Fundamentals of Biochemistry: Life at the Molecul…

Biochemistry

ISBN:

9781118918401

Author:

Donald Voet, Judith G. Voet, Charlotte W. Pratt

Publisher:

WILEY

Biochemistry

ISBN:

9781305961135

Author:

Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Fundamentals of General, Organic, and Biological …

Biochemistry

ISBN:

9780134015187

Author:

John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson

Publisher:

PEARSON

SEE MORE TEXTBOOKS