5) In an experiment to investigate the inhibition of the enzyme-glucosidase the following data for the ratesof reaction with glucopyranoside for various substrate concentrations was obtained. By constructing aLeaver-Burk plot, determine the value of the Michaelis constant.[S]/ (10-6 mol dm-3)v/ (10-3 mol dm-3 s-1)1.002.003.004.0016.733.341.149.8

Lineweaver-Burk Plot: This plot is also called as double reciprocal plot as equation for the plot is…

Answered: 5) In an experiment to investigate the…

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

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What is the reduction potential for the half-reaction Al3+(aq) + 3e Al(s) at 25°C if [A13+] = 0.44 M and E° -1.66 V? -1.66 V O-1.65 V O-1.84 V O-1.72 V O-1.67 V
If your initial absorbance from undiluted crude dialysate is 4.50, determine the fold dilution needed to yield an absorbance of approximately 0.700. If you want to prepare 1.0 ml of diluted crude, what volume (mL) of crude dialysate must you add? Your Answer: Answer units It is possible to estimate the molar extinction coefficient of a protein from knowledge of its amino acid composition, as shown from your experiences with EXPASY. From the molar extinction coefficient of tyrosine, tryptophan and cystine (cysteine does not absorb appreciably at wavelengths >260 nm, while cystine does) at a given wavelength, the extinction coefficient of the native protein in water can be computed using the following equation: e(Protein) = #(Tyr)*E(Tyr) + #(Trp)*E(Trp) + #(Cystine)*E(Cystine) Where (if A280 measured in water): E (Tyr) = 1490, ɛ (Trp) = 5500, e (Cystine) = 125 Estimate the molar extinction coefficient of lysozyme using the above equation and the amino acid composition data you found…
A galvanic cell at a temperature of 25.0 °C is powered by the following redox reaction: 2+ 2+ Sn(aq) +Ba(s) → Sn (s) + Ba** (aq) 2+ 2+ Suppose the cell is prepared with 7.71 M Sn in one half-cell and 5.89 MBa in the other. Calculate the cell voltage under these conditions. Round your answer to 3 significant digits.
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Determine the net charge on the following pentapeptide "Lys-Ala-His-Asp-Ser" at: a. pH 1.0 b. pH 10.1
This is a visible spectra between 390-590 nm obtained during the protein separation process of haemoglobin and cytochrome c using CM Sephadex chromatography. I'd like the results shown on the image interpreted. Look for characteristic peaks or patterns that correspond to the absorption properties of these proteins in the visible range.
2.1 Estimate the solubility of calcium carbonate at 25°C in the presence of 0.02M CaCl2(aq). 2.2 Will BaSO4 precipitate from a solution containing 2.5 x10 M Ba*2, barium ion, if enough soluble salt, Na2SO4, is added to make the solution 2.5 x104 M in SO42?
Given that the AG" values for the hydrolysis of glucose 1-phosphate and glucose 6-phosphate are approximately -21 kJ/mol and –14 kJ/mol, respectively, which statement is true regarding the isomerization shown? glucose 1-phosphate → glucose 6-phosphate O The reaction can likely proceed in either direction and will therefore depend on the concentrations of glucose 1-phosphate and glucose 6-phosphate. O Only the anabolic direction will occur because the free energy change is positive. O The reaction will proceed in both directions simultaneously. This reaction can only proceed in one direction and must be the rate limiting reaction for this point in metabolism.
Acetic acid is the principal ingredient in vinegar as shown; that's why it tastes sour. At equilibrium, a solution contains [CH3CO2H] = 0.0787 M and [H3 O+] = [CH3 CO2−] = 0.00118 M. What is the value of Ka for acetic acid?
Draw the Mchelis Menton plot and the Line Weaver Burk Plot using the data given below and find the Vmax and Km from the Plot.
The isoelectric point (pI) of 6-phosphogluconate dehydrogenase is 6.0. Explain why the buffer used in DEAE cellulose chromatography must have a pH greater than 6 but less than 9 in order for the enzyme to bind to the DEAE resin.
Chymotrypsin is an enzyme that is optimized to function in the small intestine (at a pH of ~7.4). Explain, given what you know about the chymotrypsin mechanism and what we learned about acid/base chemistry, why chymotrypsin would not be able to initiate catalysis if it were secreted into the stomach (pH ~2.5).

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