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IIUne UI the above äre true 4. What is the starting point for selection of a suitable ion-exchange chrom for purification of a recombinant protein? a. Prediction of isoelectric point (pl) from the amino acid sequence b. Test protein binding to an ion-exchange matrix at a range of pH: concentrations. c. Test protein binding to a selection of anion and cation exchange d. Pass your sample through a preparative column and elute with a e. Calculation of net charge from the amino acid sequence. 5. The unfolding rate of a protein in the absence of denaturant is ~10 s-l. T the protein is 2 x 10° s-'. If we assume that the system is a two-state fold is the conformational stability (in kJ mol- at 25°C) for the protein? а. 25 b. 10 с. 15 20 е. 30 6. An enzymatic reaction has a Vmax of 20 min'. At a substrate concentrati velocity of the reaction is 20 min-. Which of the following is most like a. the Km of the reaction is much less than 50 µM b. the Km of the reaction is much greater than 50 µM the Km of the reaction is equal to 50 µM d. the Km of the reaction is equal to 25 µM e. cannot be determined from the information given е.

IIUne UI the above äre true 4. What is the starting point for selection of a suitable ion-exchange chrom for purification of a recombinant protein? a. Prediction of isoelectric point (pl) from the amino acid sequence b. Test protein binding to an ion-exchange matrix at a range of pH: concentrations. c. Test protein binding to a selection of anion and cation exchange d. Pass your sample through a preparative column and elute with a e. Calculation of net charge from the amino acid sequence. 5. The unfolding rate of a protein in the absence of denaturant is ~10 s-l. T the protein is 2 x 10° s-'. If we assume that the system is a two-state fold is the conformational stability (in kJ mol- at 25°C) for the protein? а. 25 b. 10 с. 15 20 е. 30 6. An enzymatic reaction has a Vmax of 20 min'. At a substrate concentrati velocity of the reaction is 20 min-. Which of the following is most like a. the Km of the reaction is much less than 50 µM b. the Km of the reaction is much greater than 50 µM the Km of the reaction is equal to 50 µM d. the Km of the reaction is equal to 25 µM e. cannot be determined from the information given е.

Chemistry
Chemistry
10th Edition
ISBN:9781305957404
Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste
Chapter1: Chemical Foundations
Section: Chapter Questions
Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...
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e. IIUne UI tHe above åre true 4. What is the starting point for selection of a suitable ion-exchange chromatography matrix for purification of a recombinant protein? Prediction of isoelectric point (pl) from the amino acid sequence. b. Test protein binding to an ion-exchange matrix at a range of pHs and salt concentrations. a. c. Test protein binding to a selection of anion and cation exchange matrices. d. Pass your sample through a preparative column and elute with a salt gradient. e. Calculation of net charge from the amino acid sequence. 5. The unfolding rate of a protein in the absence of denaturant is ~10 s-l. The refolding rate of the protein is 2 x 105 s-l. If we assume that the system is a two-state folding process, what is the conformational stability (in kJ mol- at 25°C) for the protein? а. 25 b. 10 с. 15 O 20 30 6. An enzymatic reaction has a Vmax of 20 min-. At a substrate concentration of 50 µM, the velocity of the reaction is 20 min-'. Which of the following is most likely true? a. the Km of the reaction is much less than 50 µM b. the Km of the reaction is much greater than 50 µM the Km of the reaction is equal to 50 µM d. the Km of the reaction is equal to 25 µM e. cannot be determined from the information given
Transcribed Image Text:e. IIUne UI tHe above åre true 4. What is the starting point for selection of a suitable ion-exchange chromatography matrix for purification of a recombinant protein? Prediction of isoelectric point (pl) from the amino acid sequence. b. Test protein binding to an ion-exchange matrix at a range of pHs and salt concentrations. a. c. Test protein binding to a selection of anion and cation exchange matrices. d. Pass your sample through a preparative column and elute with a salt gradient. e. Calculation of net charge from the amino acid sequence. 5. The unfolding rate of a protein in the absence of denaturant is ~10 s-l. The refolding rate of the protein is 2 x 105 s-l. If we assume that the system is a two-state folding process, what is the conformational stability (in kJ mol- at 25°C) for the protein? а. 25 b. 10 с. 15 O 20 30 6. An enzymatic reaction has a Vmax of 20 min-. At a substrate concentration of 50 µM, the velocity of the reaction is 20 min-'. Which of the following is most likely true? a. the Km of the reaction is much less than 50 µM b. the Km of the reaction is much greater than 50 µM the Km of the reaction is equal to 50 µM d. the Km of the reaction is equal to 25 µM e. cannot be determined from the information given
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