Biochemistry 410/411 Textbook - 5th Edition - Custom Texas A&M University
5th Edition
ISBN: 9781119302940
Author: Voet
Publisher: WILEY C
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Chapter 25, Problem 5E
Summary Introduction
To explain: The reason why it is important for DNA polymerase to accommodate an A-type helix.
Introduction: DNA polymerase is a key enzyme that participates in the
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Draw a diagram to demonstrate 3' to 5' exonuclease activity?
1. Write the piece of mRNA that would code for the amino acid sequence NH3 - met - tyr - cys- his- CO2. Label the 5' and 3' ends. (diagram attached)
2.
You were tasked with purifying an untagged transcription factor (molecular weight 65,000Da, isoelectric point unknown) from a contaminant Protein A (molecular weight 50,000 Da, isoelectric point 5.0). You were also instructed to use the protein for crystallization studies after purification.i) In the initial purification step, which type of chromatography should you attempt? Explain your choice and specify the requirements of the buffer solution you should use. ii) Analyzing the proteins recovered from step i) using SDS-PAGE, you still observed a faint band of Protein A in addition to the transcription factor band. Given the limited time available for further purification, you must choose ONE appropriate chromatography method to maximize the chances of separating the two proteins as well as your crystallization studies. Provide a detailed explanation of your selection and the techniques/strategies you would employ to achieve this.
Chapter 25 Solutions
Biochemistry 410/411 Textbook - 5th Edition - Custom Texas A&M University
Ch. 25 - Prob. 1ECh. 25 - Prob. 2ECh. 25 - 3. You have discovered a drug that inhibits the...Ch. 25 - Prob. 4ECh. 25 - Prob. 5ECh. 25 - Prob. 6ECh. 25 - Prob. 7ECh. 25 - Prob. 8ECh. 25 - Prob. 9ECh. 25 - Prob. 10E
Ch. 25 - Prob. 11ECh. 25 - Prob. 12ECh. 25 - Prob. 13ECh. 25 - Prob. 14ECh. 25 - Prob. 15ECh. 25 - Prob. 16ECh. 25 - Prob. 17ECh. 25 - Prob. 18ECh. 25 - Prob. 19ECh. 25 - Prob. 20ECh. 25 - Prob. 21ECh. 25 - Prob. 22ECh. 25 - 23. Certain sites in the E. coli chromosome are...Ch. 25 - Prob. 24ECh. 25 - Prob. 25ECh. 25 - Prob. 26ECh. 25 - Prob. 27ECh. 25 - Prob. 28ECh. 25 - Prob. 29ECh. 25 - Prob. 30ECh. 25 - Prob. 31ECh. 25 - Prob. 32ECh. 25 - Prob. 33ECh. 25 - Prob. 34ECh. 25 - Prob. 35CQCh. 25 - Prob. 36CQCh. 25 - Prob. 37CQCh. 25 - Prob. 38CQCh. 25 - Prob. 39CQCh. 25 - Prob. 40CQCh. 25 - Prob. 41CQCh. 25 - Prob. 42CQCh. 25 - 43. Deinococcus radiodurans, which the Guinness...Ch. 25 - Prob. 44CQCh. 25 - Prob. 1MTE
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- Patients with pyruvate dehydrogenase deficiency show high levels of lactic acid in the blood. However, in some cases, treatment with dichloroacetate (DCA), which inhibits the kinase associated with the pyruvate dehydrogenase complex, lowers lactic acid levels. How does DCA act to stimulate pyruvate dehydrogenase activity? DCA activates pyruvate dehydrogenase kinase. DCA increases phosphorylation levels of pyruvate dehydrogenase. DCA inhibits pyruvate dehydrogenase kinase. ODCA activates pyruvate dehydrogenase phosphatase. What does this suggest about pyruvate dehydrogenase activity in patients who respond to DCA? The pyruvate dehydrogenase complex is active only when phosphorylated by the kinase. The pyruvate dehydrogenase complex is active only in the presence of the kinase. The pyruvate dehydrogenase complex is completely inactive. The pyruvate dehydrogenase complex displays some residual activity.arrow_forwardThe reduced coenzymes generated by the citric acid cycle donate electrons in a series of reactions called the electron-transport chain. The energy from the electron-transport chain is used for oxidative phosphorylation. Which compounds donate electrons to the electron- transport chain? H₂O NADH பப NAD+ ATP ADP FADH₂ FAD Which compounds are the final products of the electron-transport chain and oxidative phosphorylation? H₂O NADH NAD+ ΠΑΤΡ Π ADP FADH₂ FAD Which compound is the final electron acceptor in the electron-transport chain? Оно NADH NAD+ ATP ADP FADH₂ FADarrow_forwardHexokinase in red blood cells has a Michaelis constant (KM) of approximately 50 μM. Because life is hard enough as it is, let's assume that hexokinase displays Michaelis-Menten kinetics. What concentration of blood glucose yields an initial velocity (V) equal to 90% of the maximal velocity (Vmax)? [glucose] = What does the calculated substrate concentration at 90% Vmax tell you if normal blood glucose levels range between approximately 3.6 and 6.1 mM? Hexokinase operates near Vmax only when glucose levels are low. Hexokinase normally operates far below Vmax. Hexokinase operates near Vmax only when glucose levels are high. Hexokinase normally operates near Vmax mMarrow_forward
- Classify each coenzyme or distinguishing characteristic based on whether it corresponds to catalytic or stoichiometric coenzymes. Catalytic coenzymes Answer Bank Stoichiometric coenzymes lipoic acid FAD used once coenzyme A regenerated thiamine pyrophosphate (TPP) NAD+arrow_forwardThe oxidation of malate by NAD+ to form oxaloacetate is a highly endergonic reaction under standard conditions. AG +29 kJ mol¹ (+7 kcal mol-¹) Malate + NAD+ oxaloacetate + NADH + H+ The reaction proceeds readily under physiological conditions. = Why does the reaction proceed readily as written under physiological conditions? The NADH produced during glycolysis drives the reaction in the direction of malate oxidation. The steady-state concentrations of the products are low compared with those of the substrates. The reaction is pushed forward by the energetically favorable oxidation of fumarate to malate. Endergonic reactions such as this occur spontaneously without the input of free energy. Assuming an [NAD+ ]/[NADH] ratio of 8, a temperature of 25°C, and a pH of 7, what is the lowest [malate]/[oxaloacetate] ratio at which oxaloacetate can be formed from malate? [malate] [oxaloacetate]arrow_forwardCalculate and compare the AG values for the oxidation of succinate by NAD+ and FAD. Use the data given in the table to find the E of the NAD+: NADH and fumarate:succinate couples, and assume that E for the enzyme-bound FAD: FADH2 redox couple is nearly +0.05 V. Oxidant Reductant " E' (V) NAD+ NADH + H+ 2 -0.32 Fumarate Succinate AG°' for the oxidation of succinate by NAD+: AG°' for the oxidation of succinate by FAD: 2 -0.03 Why is FAD rather than NAD+ the electron acceptor in the reaction catalyzed by succinate dehydrogenase? The electron-transport chain can regenerate FAD, but not NAD+. FAD is an oxidant, whereas NAD+ is a reductant. The oxidation of succinate requires two NAD+ molecules but only one FAD molecule. The oxidation of succinate by NAD+ is not thermodynamically feasible. kJ mol-1 kJ mol-1arrow_forward
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