and Permease under The conditions of with and without lactose with a + or - ("+" = preser absent). Is is a mutant that cannot recognize allolactose B-Galactosidase Permease No Lactose Lactose + No Lactose Lactos +P+ O+ Z+ Y+ s P+ O-Z+Y+ + P- O+ Z- Y+
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Indicate the presence of the the B galactosidase and permease. Please explain and follow the instructions in the picture
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- For the genotypes and conditions (lactose present or absent) shown in the following Table 2, predict whether the expression of beta-galactosidase is inducible (I), noninducible (N) or constitutive (C). Explain your reason. Table 2 Genotype I*p*O°z* Condition (i) No lactose (ii) I*P*O*Z+ Lactose I*P-0*Z* (iii) (iv) Lactose ISP+O°Z+ Lactose (v) Ip*o°Z+ No lactoseFor each of the following genotypes, explain how mutation (identified by a (-) will affect the organism grown in lactose medium. Indicate whether a) B-galactosidase will be synthesized or not, b) synthesis of B-galactosidase is inducible (1) or constitutive (C) and c) growth of the organism will occur or not. i. I+P+0-Z+Y+A+/l+P+O+Z-Y-A- ii. I-P+0+Z+Y+A+/I+P-O+Z+Y+A+The intermediates A, B, C, D, E, and F all occur inthe same biochemical pathway. G is the product of thepathway, and mutants 1 through 7 are all G−, meaningthat they cannot produce substance G. The followingtable shows which intermediates will promote growthin each of the mutants. Arrange the intermediates inorder of their occurrence in the pathway, and indicatethe step in the pathway at which each mutant strain isblocked. A + in the table indicates that the strain willgrow if given that substance, an O means lack of growth.SupplementsMutant A B C D E F G1 + + + + + O +2 O O O O O O +3 O + + O + O +4 O + O O + O +5 + + + O + O +6 + + + + + + +7 O O O O + O +
- For E. coli strains with the lac genotypes show below, use a plus sign (+) to indicate the synthesis of β-galactosidase and permease and a minus sign (–) to indicate no synthesis of the proteins.TPCK and TLCK are irreversible inhibitors of serine proteases. One ofthese inhibits trypsin and the other chymotrypsin. Which is which? Explainyour reasoning. Suggest the effects of each of the following mutations on the physiologicalrole of chymotrypsinogen:(a) R15S(b) C1S(c) T147SThe proximal histidine residues have been replaced by glycine residues by mutation of the cloned genes for both the α and β subunits of hemoglobin. With the tetrameric mutant hemoglobin (all subunits being mutant, α H F8 G, β H F8 G), it was found that the “proximal” coordination bonds to hemes in the mutant protein could be replaced by having the small molecule imidazole in the buffers. Oxygen binding curves for the tetrameric mutant hemoglobin were measured. A. The degree of cooperativity in oxygen binding for the mutant hemoglobin (with imidazole present) would be expected to 1) increase 2) decrease 3) not be affected) compared with the normal protein. B. Justify your answer to part A in terms of what you know about the structural basis of cooperativity in hemoglobin. C. How would the Hill coefficient for the mutant be expected to change compared with nH for normal hemoglobin, which is ~3?
- The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of β-Dglucose to D-glucono-δ-lactone. This enzyme is highly specific for the β anomer of glucose and does not affect the α anomer. In spite of this specificity, the reaction catalyzed byglucose oxidase is commonly used in a clinical assay for total blood glucose—that is, for solutions consisting of a mixture of β- and α-D-glucose. What are the circumstances required to make this possible? Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over Fehling’s reagent for measuring blood glucose?A Leu →Ala mutation at a site buried in the core of the enzyme lysozymeis found to be destabilizing. Explain the observed effect of this mutationon lysozyme stability by predicting how enthalpy (ΔH°), conformationalentropy (ΔS°peptide), and the hydrophobic effect (ΔS°solvent) are expected to change for the mutant compared to wild-type lysozyme. Explain how ΔG°for unfolding is affected by your predicted changes in enthalpy or entropy.What fragments can be obtained from the treatment of Pro-Lys-Gly-Gly-Arg-Trp-His-Cys with trypsin and chymotrypsin simultaneously?
- 1 2 Glycogenin is a homodimer of 37 kDa subunits. (Homodimer means identical subunits of type a that form a dimer of type a2). Glycogenin has a chain of a(1,4)-linked units of glucose attached to the sidechain of a tyrosine residue. The chain of a(1,4)-linked glucose units is a primer for the initiation of glycogen synthesis by glycogen synthase. Assume the dimer is stable and not in equilibrium with monomer subunits. Which of the answers below are plausible pathways for attaching or building the primer chain of glucose units? The branching enzyme attaches a chain of 7 glucose units to the tyrosine sidechain of glycogenin. 0 0 0 0 000 The transferase attaches 3 units of a(1,4)-linked glucose to the tyrosine sidechain of glycogenin. Glycogen synthase then extends the chain using UDP-Glc. 0 One glycogenin dimer builds the a(1,4)-llinked glucose chain on a subunit of another glycogenin dimer. -D-O Each subunit builds the a(1,4)-Ilinked glucose chain on the other subunit of the same dimer.…The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of B-D-glucose to D-glucono-6-lactone. The enzyme is highly specific for the B anomer of glucose and does not affect the a anomer. In spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose -that is, for solutions consisting of a mixture of B- and a-D-glucose, as well as other sugars present in blood. The oxidation proceeds in the presence of oxygen and forms hydrogen peroxide, in addition to the lactone. A second enzyme, called peroxidase, catalyzes the reaction of hydrogen peroxide with colorless compounds to create a colored product, which is quantified with a simple spectrophotometer. What are the circumstances required to make this possible? Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over the Fehling's reagent for measuring blood glucose?Why is the position of Cys 58 important in 3GRS(GLUTATHIONE REDUCTASE)? When Cys 58 is mutated to GLY 58 how would it impact the 3D structure and function of 3GRS? explain in terms of how Cys and GLY have different properties and how it would impact the function of 3GRS (the binding sites etc.) You can see your structure(3GRS ) here or any other website: https://www.rcsb.org