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- Give Explanation Detailed Solution of sub parts..(no need handwritten answer)2. The following tyrosine-phosphorylated polypeptides were tested as substrates of protein tyrosine phosphatase, an important enzyme in cellular signal transduction. The pTyr in bold signifies the tyrosine residue that is phosphorylated. The binding affinities of the polypeptide substrates to the enzyme were found to follow the order: (a) > (c) - (d) >> (b). (a) Asp-Ala-Asp-Glu-pTyr-Leu-lle-Pro-Gln-Gln-Gly (b) Pro-Val-Pro-Glu-pTyr-lle-Asn-Ala-Ser-Val (c) Asp-Ala-Glu-Glu-pTyr-Leu-Val-Pro-Gln-Gln-Gly (d) Asp-Asn-Leu-Tyr-pTyr-Trp-Asp-Glu-Asn-Ser-Ser In addition to the presence of the phosphorylated tyrosine residue, what amino acid a) properties of the polypeptides accounts for the relative order of binding affinities to the enzyme? b) the active site of the phosphatase enzyme that are responsible for the affinity of substrate binding? Assume a pH of 7.4 at the enzyme active site. (Note a phosphatase uses phosphate substrate) What amino acids have side chains that would indicate they are…In what type of intra and intermolecular interactions does a valine within a protein backbone typically participate? How would this variation in Sickle Cell Disease be classified?
- 19. Define the terms “cofactor” and “coenzyme.” 20. What is the difference between general acid-base catalysis and specific acid-base catalysis? (Assume that the solvent is water.)7. [10'] For a bacteriophage 77, the following data at zero concentration have been obtained: Sedimentation coefficient: $20,w = 453 S. Diffusion coefficient: D₂0. = 6.03×10-8 cm² s¹¹. 20,w Specific volume V20 = 0.639 cm³ g¹ Calculate the molecular mass M of the bacteriophage.Antithrombin III forms an irreversible complex with thrombin but not with prothrombin. What is the most likely reason for this difference in reactivity?
- 1. Researchers isolated a monomeric protein from platelets that has 2 binding sites (A and B) for ADP; Site A's Ka is 157 μM, and Site B's Kd is 2.2 μM. 1.1. A) Which binding site has higher affinity for ADP? B) Briefly justify your answer. C) For this higher affinity site, calculate the standard free energy change for ADP binding. Show your work. 1.2. What concentration of ADP is required to get site A filled in 20% of the proteins? 1.3. Based on this information, sketch a graph of the fraction of site B filled as a function of [ADP].A one-to-one protein (P)-ligand (L) complexation (P + L PL) has a dissociation equilibrium constant (Kd) value of 100 nM at 25°C, and the Kd remains the same at 37°C. 1) What is AS of binding at 25°C? Assume ACp of the binding is 0 over the temperature range. AS = 1.34E2 kJ/(mol*K) (note the unit!!) (sig. fig =3) 2) What is the concentration of the PL complex formed at equilibrium when you mix 0.20 uM (microM) of Protein and 1.0 uM of Ligand together at 37°C? PL at equilibrium = 8.1E-1 uM (note the unit!!) (sig. fig =2)VI. Although most biologically relevant sugars have the D-configuration, L-fucose is a commonly observed monosaccharide component in glycoproteins. Glycosylated antibodies (IgGs) observed in patients with active TB have more fucose than those found in patients with latent TB (Lu et. al., 2016). Latent TB occurs when a person has the TB bacteria, but bacterial proliferation is kept under control by the body's immune system; hence, the infected person is asymptomatic and not infectious. A person with latent TB will test positive for the tuberculin test or TB blood test. a) L-fucose is also known as 6-deoxy-L-galactose. Note that D-galactose is a C-4 epimer of D-glucose. Draw the Fisher projections for D-glucose, D-galactose and L-fucose. (Hints: D- and L-isomers are enantiomers. 6-deoxy means that the hydroxyl group at C-6 is removed leaving just the methyl group). D-galactose: D-glucose: L-fucose (6-deoxy-L-galactose): b) L-fucose can cyclize into a pyranose and form two anomers. Draw…
- 29. In sickle cell anemia, a hereditary disease, there is substitution of one amino acid by another in one of the four polypeptide chains of hemoglobin. In this case are all of the structural levels of the protein modified?5. Anesthetic gases used in surgery are known to bind to the hemoglobin molecule in red blood cells. The diagram below illustrates O2 binding curves of normal human HbA in the presence of the anesthetic gas dichloromethane (DCM). O UNTREATED 100 a Dсм 23 Torr Symbols: в Dсм 50 Torr x DCM I00 Torr o, 0 Torr DCM; O, 23 Torr DCM A, 50 Torr DCM x, 100 Torr DCM. 80 60 40 (1 Torr = 1 mm Hg.) 20 The solutions were buffered to pH 7.4. 0.5 1.0 1.5 2.0 log p02 (a) (* Hill plots. Label the axes and indicate on both the plot above and the Hill plot where the value of the dissociation equilibrium constant Ka for O2 binding is defined for 0 and 100 Torr of dichloromethane For the curves at 0 and 100 Torr of dichloromethane, draw their equivalent in the form of Kd Hb(O2)n Hb + nO2 % OXYGENATION. In principle, an allosteric molecule could exhibit negative coopera- tivity; that is, binding of the first ligands could decrease affinity for additional ones. (a) What would a Hill plot look like for negative cooperativity? (b) It has been noted that the KNF theory allows negative coopera- tivity but the MWC theory doesn't. Explain.