dissociation constant, Kd, for a particular repressor-operator complex is approximately 10-¹1 M. The An E. coli cell with a volume of 2.0 x 10-¹2 mL contains 10 copies of the repressor. Calculate the cellular concentration of the repressor protein inside the cell. repressor protein concentration = Number M Given the concentration of repressor protein and its Kd value, select the statement below that is most likely correct.

dissociation constant, Kd, for a particular repressor-operator complex is approximately 10-¹1 M. The An E. coli cell with a volume of 2.0 x 10-¹2 mL contains 10 copies of the repressor. Calculate the cellular concentration of the repressor protein inside the cell. repressor protein concentration = Number M Given the concentration of repressor protein and its Kd value, select the statement below that is most likely correct.

Principles of Instrumental Analysis

7th Edition

ISBN:9781305577213

Author:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Publisher:Douglas A. Skoog, F. James Holler, Stanley R. Crouch

Chapter14: Applications Of Ultraviolet-visible Molecular Absorption Spectrometry

Section: Chapter Questions

Problem 14.13QAP: Copper(II) forms a 1:1 complex with the organic complexing agent R in acidic medium. The formation...

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Copper(II) forms a 1:1 complex with the organic complexing agent R in acidic medium. The formation ofthe complex can be monitored by spectrophotometry at 480 nm. Use the following data collected under pseudo-first-order conditions to construct a calibration curve of rate versus concentration of R. Find the concentration of copper(II) in an unknown whose rate under the same conditions was 6.2 10- 3A s-1.
The kinetics of an enzyme are measured as a function of [S] in the presence and absence of 2 mM I. Compute Km and Vmax in the absence and presence of I S] (uM) V (uM/min) without I with I 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8
The enzyme-catalysed conversion of a substrate at 298 K has KM = 0.032 mol dm−3 and vmax = 4.25 × 10−4 mol dm−3 s−1 when the enzyme concentration is 3.60 × 10−9 mol dm−3. Calculate the catalytic efficiency of the enzyme, as defined in Exercise E17F.5(a).
An enzyme catalyzes a reaction with a KmKm of 7.507.50 mM and a VmaxVmax of 3.00 mM⋅s−1.3.00 mM⋅s−1. Calculate the reaction velocity, v0,v0, for each substrate concentration. a. [S]=4.00mM*s^-1 b. [S]=7.5mM*s^-1
An enzyme-catalyzed reaction has a Km of 1 mM and a Vmax of 4 nmole/L sec-1. The reaction velocity (nmole/L sec-1) when the substrate concentration is 0.25 mM is: A. 1.25 B. 10.0 C. 5.0 D. 0.50 E. 1.0 F. 100 G. 150 H. 55 I. 75
Determine the value of the turnover number of the enzyme catalase, given that RmaxRmax (Vmax)(Vmax) for catalase is 41 mmol⋅L−1⋅s−141 mmol⋅L−1⋅s−1 and [E]t[E]t equals 4.8 nmol⋅L−14.8 nmol⋅L−1 . Catalase has a single active site.
Many enzymes are inhibited irreversibly by heavy metal ions such as Hg2+, Cu2+, or Ag+, which can react with essential sulfhydryl groups to form mercaptides:The affinity of Ag + for sulfhydryl groups is so great that Ag+ can be used to titrate —SH groups quantitatively. To 10.0 mL of a solution containing 1.0 mg/mL of a pure enzyme, an investigator added just enough AgNO3 to completely inactivate the enzyme. A total of 0.342 μmol of AgNO3 was required. Calculate the minimum molecular weight of the enzyme. Why does the value obtained in this way give only the minimum molecular weight?
An enzyme-catalyzed reaction has a Km of 1.4 mM and a Vmax of 7 nM/s. What is the initial velocity when the substrate concentration is 0.6 mM?
The equilibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200. In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1. What is the rate constant for the loss of the unreacted substratefrom the active site?
. A student collects the following data for the absorbance of a complex measured in 1.00 cmspectrophotometric cells. The molar absorptivity (ε) of the complex under investigation is 2.25×103L/mol·cm. Calculate the concentration of the complex in solution at each time of the reaction.Time (min)MeasuredAbsorbanceComplex Concentration(M)0.000 1.50010.000 1.31320.000 1.12530.000 0.93840.000 0.750
The following data were obtained on the initial rates of reaction of a d-metal complex in aqueous solution. For the experiments a. [Y] = 2.7 mmol/dm3, and for experiments b. [Y] = 6.1 mmol/dm3 Conc. complex/(mmol dm-3) 8.01 9.22 12.11 Exp. a. v/ (mol dm-3 s-1) 125 144 190 Exp. b. v/ (mol dm-3 s-1) 640 730 960 (a) What is the order of reaction with respect to the complex AND the reactant Y. Choose one. (b) use the data above to calculate the rate constant. k = ________ (mol/L/s, s-1, L/mol/s, or L2/mol2/s). 3 s.f. normal format.
The following data were obtained on the initial rates of reaction of a d-metal complex in aqueous solution. For the experiments a. [Y] = 2.7 mmol/dm3, and for experiments b. [Y] = 6.1 mmol/dm3 Conc. complex/(mmol dm-3) 8.01 9.22 12.11 Exp. a. v/ (mol dm-3 s-1) 125 144 190 Exp. b. v/ (mol dm-3 s-1) 640 730 960 (a) What is the order of reaction with respect to the complex AND the reactant Y. (b) use the data above to calculate the rate constant. k = ________ (mol/L/s, s-1, L/mol/s, or L2/mol2/s). 3 s.f. normal format.