I need help with numbers 2,6 & 8 Chapter 8 Biomolecular Interactions: Ligand Bin

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I need help with numbers 2,6 & 8 Chapter 8 Biomolecular Interactions: Ligand Binding and Enzyme Reactions 263 0.36 0.43 0.68 1.08 1.63 1.83 1.95 1.98 0.60 2.4 3.6 4.8 6.0 One of the many straight-line modifications of the Michaelis-Menten equation is the Eadie-Hofstee equation: Beginning with the Lineweaver-Burk equation, derive the Eadie-Hofstee equation. Explain how it may be used to plot a straight line from experimental rate data. How are Vmax and KM calculated? 3. A research project you are working on involves the study of sugar binding to human albumin. The sugars to be tested are not fluorescent, and you do not wish to use a sec- ondary probe such as a dye. Human albumin has only one tryptophan residue, and you know that this amino acid is fluorescent. You find that the tryptophan fluorescence spectrum of human albumin undergoes changes when various sugars are added. Can he finding? u explain the results of this experiment and discuss the significance of t 4. Equation 8.6 in this chapter can be used to determine Ky values, but hyperbolic plots are obtained. Convert Equation 8.6 into an equation that will yield a linear plot with- out going through all the changes necessary for the Scatchard equation. Hint: See the Michaelis-Menten equation and the Lineweaver-Burk equation. 5. You are attempting to develop a colorimetric probe for use in binding studies List several requirements that the probe must meet in order to be effective. For exam- ple, it must bind at specific locations of the macromolecule. Can you think of other 6. Using the data in Problems 7 and 8, calculate the specific activity of the enzyme in g. Assume the enzyme has a molecular weight of 55,000 and uirements? units/mg and katal/mg the reaction mixture for each assay is contained in a total volume of 1.00 mL. corresponding substrate concentration. Use any graphical method or computer pro- gram to determine kM and Vmax 7. The table below gives initial rates of an enzyme-catalyzed reaction, along with the o aM/min) 130 116 87 [S) (mole/liter) 65 × 10-5 23 × 10-5 79 x 10-5 3.9× 10-5

Explanation / Answer

2.

6.

Vmax = 1/7150.4 = 1.3 x 10-4 mole/min

Km/Vmax = 0.3428

Km = 0.3428 x 1.3 x 10-4= 0.44 x 10-4moles

8.

S (mole/liter v (mole/min) 1/s 1/v 65 × 10-5 0.00013 1538 7692.308 23 × 10-5 0.000116 4347 8620.69 7.9 × 10-5 0.000087 12658 11494.25

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