Indicate the mechanism of enzyme inhibition represented in each plot, and justify your answer with respect to inhibitor effect on Km and Vm

Q: binding dissociation constant can experimentally be determined by knowing: O The ligand…

A: The solution is shown below.

Q: Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following…

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Q: Which type of inhibitor is shown in the diagram? non-competitive inhibitor uncompetitive inhibitor…

A: Given options,         Non-competitive inhibitor         Uncompetitive inhibitor         All…

Q: We have three inhibitor and same enzyme were incubated with 5 mM of substrate and 2 mM of…

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Q: In carbonic anhydrase II, Zn* acts as a Lewis acid coordinated in the enzyme active site to…

A: This statement is False. carbonic anhydrase is an enzyme used to increase  the rate  of equilibrium…

Q: Calculate the value of the denaturation constant kd for a given enzyme, using the equation provided…

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Q: Use the equations of the lines plotted in regards to the data pictured to determine Km and Vmax in…

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Q: Which substrate concentration range is best for determining the catalytic efficiency of an enzyme…

A: In enzyme catalyzed reaction the catalytic effeciency is defined as how efficiently enzyme converts…

Q: Which of the following conditions would be best to get an enzyme with a pl of 7.0 to stick to a…

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Q: To the right is a Michaelis-Menten plot for a wildtype enzyme (STCS) and three different mutants.…

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Q: se inhibitors were s

A: Log1/C = Measure of Biological activity

Q: 7. In the biosynthesis of proteins it is important that the correct tRNA binds to its corresponding…

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Q: Given the following data in enzyme-catalyzed reaction, what is the Vm, Km and type of inhibition of…

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Q: Concentration, uM Vo (umol/min) w/o Vo (umol/min) with substance B substance B 0.4 0.08 0.069 0.7…

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Q: Noncompetitive inhibition is a limiting case in which the effect of binding inhibitor has no effect…

A: Enzyme inhibitors are of two types depending on their enzyme action They are as follows 1.…

Q: A medicinal chemist is trying to determine the mechanism of action of inhibitors she has…

A: Since you have asked multiple questions, we will solve the first question for you. If you want any…

Q: A particular enzyme's activity is low at high pH but increases at lower pH. These data suggest that…

A: Since you have asked multiple question, we will solve the first question for you. If you want any…

Q: What is responsible for the large range in values of dissociation constants listed in Table 2.18?

A: In the above given types of bio affinity interactions there are different types of intermolecular…

Q: 8. Identify the inhibitor from the following list for the selective target of the enzyme having C in…

A: o Acrylamide groups act as Michael acceptors and thus react with nucleophiles like thiol (SH) groups…

Q: Describe the differences between chain termination, chain transfer and inhibition. Use suitable…

A: chain termination :  Polymerization of many radical reactions involve chain reactions or chain…

Q: CH Vacant d-orbital of metal

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Q: At what substrate concentration would an enzyme with a kcat of 30.0 s-1 and a Km of 3. (а) 0.0050 M…

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Q: Two phenylalanine residues are separated by 1.0 nm in a polypeptide. Calculate the dispersion…

A: Dispersion force is the force of attraction that exist between atoms or molecules that developed…

Q: 7. 116.5 ug of trypsin (MW 23.3 kDa) was mixed in a l ml solution with an excess of a peptide…

A: Hello. Since your question has multiple sub-parts, we will solve the first three sub-parts for you.…

Q: . TPCK and TLCK are irreversible inhibitors of serine proteases. One of these inhibits trypsin and…

A: Irreversible inhibitor for chymotrypsin is Tosyl phenylalanyl chloromethyl ketone (TPCK) because it…

Q: Which protein folding interaction(s) is/are most likely to occur on the outside of a protein pocket…

A: Hydrophobic effects describe the energetic preference of non polar molecular surfaces interacting…

Q: The biuret reaction is a general method for the determination of proteins or peptides. This method…

A: Beer-Lambert law studies the relation between the concentration and absorbance in a sample.…

Q: The KM of an enzyme is 2.5 mM, In the presence of 2 mM of an inhibitor, the intercept at the (1/[S])…

A: Given observation For an enzyme catalyzed reaction In presence of inhibitor ,the intercept at 1/[S]…

Q: The following diagram illustrates the process of fragment-based drug discovery Binding site her…

A: In the development of drug, it is necessary that drug must be attached to binding site. Only a…

Q: 2. The kinetics of an enzyme are measured as a function of substrate concentration in the presence…

A: Since you have asked multiple questions, we will solve the first question for you. If you want any…

Q: The following is a plot form an enzyme with and without an inhibitor. Utilizing your knowledge of…

A: Competitive inhibitors bind to the active site of the enzyme and thus compete with the substrate in…

Q: Following data were obtained for an enzyme in the absence and presence of an inhibitor. What are the…

A: Given data:

Q: Would the continuous assay of Alkaline phosphatase (kinetics lab) with PNPP as a substrate work if…

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Q: How can distance validate non-covalent interactions? Also, please explain if the distance between…

A: Non-covalent interaction: It is a weaker force of attraction than covalent interaction. Molecules…

Q: What is the relative activite and the degree of inhibition caused by a competitive inhibitor when…

A: Degree of inhibition The introduction of an internal control—the rate of the uncontrolled…

Q: Is the inhibitor competitive, uncompetitive or non competitive and why?

A: Competative inhibiton- The inhibitor Binds only free enzyme. Binding occur only free enzyme. Non…

Q: PLEASE ANSWER THIS

A: Lineweaver-Burk plot is usually taken as double reciprocal plots. It is a graphical method which is…

Q: If inhibitor X changes lactase activity to a Vo of 0.10 mM per minute when [S] = 1.0 mM, and a Vo of…

A: Given: Reaction velocity (V0)1 = 0.10 mM/min [S]1 = 1.0 mM Reaction velocity (V0)2 = 0.133333 mM/min…

Q: E. coli S. aureus B. cereus Antibiotic Zone Size Susceptibility Zone Size Susceptibility Zone Size…

A: Zone size of inhibition is defined as a circular area around the spot of the antibiotic in which…

Q: Find the apparent Km and apparent Vmax for the enzyme reaction containing the inhibitor and identify…

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Q: what are the advantages of mediator-based amperometric enzyme sensors for glucose compred to…

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Q: Protein phosphatase 1 (PP1) helps regulate cell division and is a possible drug target to treat…

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Q: Asparagine and glutamine residues in proteins are deamidated in an aqueous solution to yield…

A: Deamidation is the conversion of amide group to another functional group. Side chain of amino acid…

Q: Calculate the slope on a Lineweaver-Burk plot (Km / Vmax) for the lactase reaction with inhibitor X.…

A: According to  Lineweaver-Burk plot, the plot between 1/V v/s 1/S gives a straight line as  1/V = M/S…

Q: The isoelectric point, pl, of the protein soybean trypsin inhibitor is 4.5 , while that of…

A: In proteins, the isoelectric point (pI) is defined as the pH at which a protein carries no net…

Q: 5. The following kinetic data are recorded for equal amounts of the enzyme, proline racemase in the…

A: Competitive inhibitors bind to the free enzyme and show changes in the slope of the plot whereas…

Q: The migration distances r, for each of the proteln standards bands and that of the unknown protein…

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Q: 1.Serine protease is one of the most studied mechanisms in biochemistry. A. Using the diagram…

A: The main player in the catalytic mechanism in the serine proteases is the catalytic triad. The triad…