BIOCHEMISTRY (LOOSELEAF) >CUSTOM PKG<
8th Edition
ISBN: 9781305760738
Author: Campbell
Publisher: CENGAGE C
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Chapter 9, Problem 51RE
Explain briefly what happens to eukaryotic mRNA before it can be translated to protein.
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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 9 Solutions
BIOCHEMISTRY (LOOSELEAF) >CUSTOM PKG<
Ch. 9 - REFLECT AND APPLY Consider the following in light...Ch. 9 - Prob. 2RECh. 9 - RECALL What is the structural difference between...Ch. 9 - RECALL Give the name of the base, the...Ch. 9 - RECALL What is the difference between ATP and...Ch. 9 - RECALL Give the sequence on the opposite strand...Ch. 9 - RECALL Are the sequences shown in Question 6 those...Ch. 9 - REFLECT AND APPLY (a) Is it biologically...Ch. 9 - REFLECT AND APPLY A friend tells you that only...Ch. 9 - REFLECT AND APPLY In the early days of molecular...
Ch. 9 - REFLECT AND APPLY Why is RNA more vulnerable to...Ch. 9 - Prob. 12RECh. 9 - RECALL Draw a GC base pair. Draw an AT base pair.Ch. 9 - RECALL Which of the following statements is (are)...Ch. 9 - Prob. 15RECh. 9 - BIOCHEMICAL CONNECTIONS Describe the landmark case...Ch. 9 - Prob. 17RECh. 9 - Prob. 18RECh. 9 - RECALL Which of the following statements is (are)...Ch. 9 - RECALL Define supercoiling, positive supercoil,...Ch. 9 - RECALL What is propeller twist?Ch. 9 - RECALL What is an AG/CT step?Ch. 9 - RECALL Why does propeller-twist occur?Ch. 9 - Prob. 24RECh. 9 - RECALL If circular B-DNA is positively...Ch. 9 - RECALL Briefly describe the structure of...Ch. 9 - Prob. 27RECh. 9 - REFLECT AND APPLY List three mechanisms that relax...Ch. 9 - REFLECT AND APPLY Explain how DNA gyrase works.Ch. 9 - Prob. 30RECh. 9 - REFLECT AND APPLY Would you expect to find...Ch. 9 - REFLECT AND APPLY One of the original structures...Ch. 9 - REFLECT AND APPLY What is the complete base...Ch. 9 - REFLECT AND APPLY Why was it necessary to specify...Ch. 9 - Prob. 35RECh. 9 - Prob. 36RECh. 9 - Prob. 37RECh. 9 - BIOCHEMICAL CONNECTIONS A recent commercial for a...Ch. 9 - REFLECT AND APPLY A technology called PCR is used...Ch. 9 - REFLECT AND APPLY Why does DNA with a high AT...Ch. 9 - Prob. 41RECh. 9 - Prob. 42RECh. 9 - Prob. 43RECh. 9 - Prob. 44RECh. 9 - 45. Why does the absorbance increase when a DNA...Ch. 9 - Prob. 46RECh. 9 - REFLECT AND APPLY Would you expect tRNA or mRNA to...Ch. 9 - REFLECT AND APPLY The structures of tRNAs contain...Ch. 9 - REFLECT AND APPLY Would you expect mRNA or rRNA to...Ch. 9 - REFLECT AND APPLY Which would be more harmful to a...Ch. 9 - Explain briefly what happens to eukaryotic mRNA...Ch. 9 - Prob. 52RE
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- 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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