Biology
5th Edition
ISBN: 9781260487947
Author: BROOKER
Publisher: MCG
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Chapter 12.5, Problem 1CS
Core Skill: Connections Look back at Figure 6.3, which describes the hydrolysis of ATP. Why is ATP needed to charge a tRNA?
Figure 6.3 The hydrolysis of ATP to ADP and Pi. As shown in this figure, ATP has a net charge of −4, while ADP and Pi are shown with net charges of −2 each. When these compounds are shown in
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Suppose you are working with a crude enzyme and the next goal is enyme purification. Explain how important physicochemical properties of that biomolecule will affect downstream processing.
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Chapter 12 Solutions
Biology
Ch. 12.1 - What disease would result if a person inherited...Ch. 12.1 - Prob. 2CCCh. 12.1 - What is the direction of flow of genetic...Ch. 12.2 - Core Skill: Connections Look back at the role of...Ch. 12.3 - Prob. 1CCCh. 12.4 - Prob. 1CCCh. 12.4 - Prob. 1EQCh. 12.4 - Prob. 2EQCh. 12.4 - Prob. 3EQCh. 12.5 - Core Skill: Connections Look back at Figure 6.3,...
Ch. 12.5 - Prob. 2CSCh. 12.6 - Prob. 1CCCh. 12 - Which of the following best represents the central...Ch. 12 - A mutation prevents a gene from being transcribed...Ch. 12 - Prob. 3TYCh. 12 - Prob. 4TYCh. 12 - If a eukaryotic mRNA failed to have a cap attached...Ch. 12 - Prob. 6TYCh. 12 - Prob. 7TYCh. 12 - During the initiation of translation, the first...Ch. 12 - Prob. 9TYCh. 12 - Prob. 10TYCh. 12 - Prob. 1CQCh. 12 - Prob. 2CQCh. 12 - Prob. 3CQCh. 12 - Prob. 1COQCh. 12 - Prob. 2COQ
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- VISUALIZE Sketch a pyrimidine nucleotide subunit that would be found only in RNA. Circle and label the three components that make up this type of nucleotide. Explain what changes in the functional groups of this subunit would have to occur for it to be found in a DNA molecule.arrow_forwardMacmillan Learning The graphs show a titration curve for the amino acid histidine. Label the fist curve with the major histidine species at each position. One histidine species will not be used. Label the second curve with the pKå values for the histidine functional groups and the isoelectric point (pI) of histidine. 14 12 10 8 HH pH 6 His [His] = [His] 2 His²- [His² +] = [His*] 0 0.0 0.5 1.0 Incorrect Answer 1.5 [OH-] (equivalents) Hisº His [His] = [His] 2.0 2.5 3.0 His² + Answer Bankarrow_forwardTopic: Biocatalysts where does the covalent modification occur, for enzymes? list 3 types of covalent modifications. what kind of change in the local properties, structure of the enzyme is cauae by covalent modification? how does this change appear in enzyme funtion?arrow_forward
- Exercise 1 Summarize the data below obtained from the protein experiments for determination of protein concentration in the form of a graph. Plot a graph containing a title and labels for both of the axis. Three readings were taken for each protein concentration. Find the averages and standard deviations for each reading and plot your graph using Microsoft EXCEL, complete with the error bars. This graph represents will be used to measure the protein concentration in an unknown protein solution. calibration curve for a protein assay (next experiment) where this Concentration of protein (Hg/mL) Absorbance, 595 nm 1 2 3 0.04 0.05 0.03 2 0.12 0.11 0.14 5 0.26 0.25 0.25 10 0.49 0.49 0.51 25 0.82 0.85 0.83 50 1.28 1.24 1.25arrow_forwardProblem: From the following information determine the amino acid sequence of a peptide. N-terminal Edman gives PTH-Alanine C terminal carboxypeptidase treatment, no observable reaction Trypsin cleavage gives three products Arg Peptide containing Ala, Lys Peptide containing Asp, Met, Phe, Pro Mild Chymotrypsin cleavage gives 2 peptides Peptide containing Asp, Pro Peptide containing Ala, Arg, Lys, Met, Phe CNBr cleavage gives 2 peptide Peptide containing Ala, Arg, Lys and homoserine Peptide containing Asp, Phe, Pro You must supply the answer as the 3-letter amino acid sequence from N-terminus to C-terminus in the form (you must use dashes, not spaces between the amino acids)arrow_forwardProblem: From the following information determine the amino acid sequence of a peptide. N-terminal Edman gives PTH-Alanine C terminal carboxypeptidase treatment, no observable reaction Trypsin cleavage gives three products Arg Peptide containing Ala, Lys Peptide containing Asp, Met, Phe, Pro Mild Chymotrypsin cleavage gives 2 peptides Peptide containing Asp, Pro Peptide containing Ala, Arg, Lys, Met, Phe CNBr cleavage gives 2 peptides Peptide containing Ala, Arg, Lys and homoserine Peptide containing Asp, Phe, Pro You must supply the answer as the 3-letter amino acid sequence from N-terminus to C-terminus in the form (you must use dashes, not spaces between the amino acids) Met-Thr-Glu-Trparrow_forward
- Protein purification table: A 50 ml crude skeletal muscle extract contains 32mg of protein per ml. Ten ul of the extract catalyzes a reaction at a rate of 0.14 µmol product per minute. The extract was fractionated by ammonium sulfate precipitation, and the fraction precipitating between 20% and 40% saturation was dissolved in 10ml. The solution contains 50mg/ml protein. Ten ul of this purified fraction catalyzes the reaction at a rate of 0.65 µmol/min (a) What is the degree of purification (fold purification)? (b) What is the percent yield of the enzyme recovered in the purification?arrow_forwardTopic: Enzyme (Prelab) Define optimum pH and temperature of an enzyme How do changes in pH and temperature affect the native conformation of an enzyme?arrow_forwardMacmillan Learning The graphs show a titration curve for the amino acid histidine. Label the fist curve with the major histidine species at each position. One histidine species will not be used. Label the second curve with the pKå values for the histidine functional groups and the isoelectric point (pI) of histidine. 14 12 10 pH 6 8 4 His²+ 2 His+ 0 0.0 0.5 1.0 Incorrect Answer His²- [His²+] = [His*] 1.5 [OH-] (equivalents) Hisº His [His]=[His] 2.0 2.5 3.0 Answer Bank [His+] = [His]arrow_forward
- Enzyme Investigation An enzyme was isolated from digestive juices taken from the small intestine. An experiment was set up to test the ability of the enzyme to break down protein. Two test tubes, labeled A and B, were placed in a hot water bath at 37°C, human body temperature. Test tube A contained only protein and test tube B contained protein and the enzyme. The chart below shows the set-up. After two hours, the contents of both test tubes were analyzed. Test tube A showed only the presence of protein. Test tube B showed the presence of the end products of protein digestion, indicating the enzyme had successfully broken down the protein. Identify the end products of protein digestion that made up the contents of test tube B after the two hours.arrow_forwardBradford technique makes use of the Coomassie blue dye that binds to the protein, with the complex absorbing strongly at 465 nm. O True O Falsearrow_forwardQuest: 22 // I had asked a bartleby tutor to help me with this question but they got it incorrect. Want to know where they went wrong?arrow_forward
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