Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 7, Problem 9P
Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.
The Effect of Carbohydrates on Proteolysis of Glycophorin (Integrates with Chapters 5n 6, and 9.) Consider the sequence of glycophorin (see Figure 9.1U), and imagine subjecting glycophorin, and also a sample of glycophorin treated to remove all sugars, to treatment with trypsin and chymotrypsin. Would the presence of sugars in the native glycophorin make ally difference to the results?
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Chapter 7 Solutions
Biochemistry
Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Prob. 10P
Ch. 7 - Prob. 11PCh. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Prob. 14PCh. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Prob. 18PCh. 7 - Prob. 19PCh. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...
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- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Determining the Branch Points and Reducing Ends of Amylopectin A 0.2-g sample of amylopectin was analyzed to determine the fraction of the total glucose residues, that are branch points in the structure. The sample was exhaustively methylated and then digested, yielding 50-mol of 2,3-dimethylgluetose and 0.4 mol of 1,2,3,6- letramethylglucose. What fraction of the total residues are branch points? I low many reducing ends does this sample of amylopectin have?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. (Research Problem) The Nature and Roles of Linear Motifs in Proteins In addition to domains and modules, there are other significant sequence patterns in proteins—known as linear motifs—that are associated with a particular function. Consult the biochemical literature to answer the following questions: 1. What are linear motifs? 2. How are they different from domains?. 3. What are their functions? 4. How can they be characterized? 5. There are several papers that are good starting points for this problem. Neduva, V., and Russell, R., 2005. Linear motifs: evolutionary interaction switches. FEBS Letters 579:3342-3345. Gibson, T., 2009. Cell regulation: determined to signal discrete cooperation. Trends in Biochemical Sciences 34:471-482. Diella, K. Haslam, N., Chica., C. et aL, 2009. Understanding eukaryotic linear motifs and their role in cell signaling and regulation. Frontiers of Bioscience 13:6580-6603.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Graphical Analysis of MWC Allosteric Enzyme Kinetics (Integrates with Chapter 1.1) Draw both Line weaver-Burk plots and Hanes-Woolf plots for an MWC allosteric enzyme system, showing separate curves for the kinetic response in (a) the absence of any effectors, (b) the presence of allosteric activator Λ, and (c) the presence of allosteric inhibitor I.arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. The Biosynthetic Capacity of Cells The nutritional requirements of Escherichia coli cells are far simpler than those of humans, yet the macromolecules found in bacteria are about as complex as those of animals. Because bacteria can make all their essential biomolecules while subsisting on a simpler diet, do you think bacteria may have more biosynthetic capacity and hence more metabolic complexity than animals? Organize your thoughts on this question, pro and con, into a rational argument. (Section 1.5)arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - I Measurement of the rate constants for a simple enzymatic reaction obeying Michaelis-Menten kinetics gave the following results: k1=2108M1sec1k1=1103sec1k2=5103sec1a. What is Ks, the dissociation constant for the enzyme-substrate complex? b. What is Km, the Michaelis constant for this enzyme? c. What is kcat (the turnover number) for this enzyme? d. What is the catalytic efficiency (kcat/Km) for this enzyme? e. Does this enzyme approach kinetic perfection? (That is, does kcat/Km approach the diffusion-controlled rate of enzyme association with substrate?) f. If a kinetic measurement was made using 2 nanomoles of enzyme per mL and saturating amounts of substrate, what would Vmax equal? g. Again, using 2 nanomoles of enzyme per mL of reaction mixture, what concentration of substrate would give v = 0.75 Vmax? h. If a kinetic measurement was made using 4 nanomoles of enzyme per mL and saturating amounts of substrate, what would Vmax equal? What would Km equal under these conditions?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Describe the Effects on cAMP and Glycogen Levels in Cells Exposed to Cholera Toxin Cholera toxin is an enzyme that covalently modifies the G-subunit of G proteins. (Cholera toxin catalyzes the transfer of ADP-ribose from NAD+ to an arginine residue in Gan ADP-ribosylation reaction.) Covalent modification of G� inactivates its GTPase activity. Predict the consequences of cholera to.vin on cellular cAMP and glycogen levels.arrow_forward
- Answers to all problems are at the end of this book Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Analysis of the blood of a catatonic football fan revealed large concentrations of a. psychologic octapeptide. Amino acid analysis of this oclapeplide gave the following results: 2 Ala lArg 1 Asp 1 Mel 2 Tyr I Val 1NH/ The following facts were observed: Partial acid hydrolysis of the octapeptide yielded a dipeptide of the structure Chymolrypsin treatment of the octapeplide yielded two tetrapeptides, each containing an alanine residue. Trypsin treatment of one of the tetrapeptides yielded two dipeptides. Cyanogen bromide treatment of another sample of the same tetrapeplide yielded a tripeplideand free Tyr. N-lerminal analysis of the other tetrapeptide gave Asn. What is the amino acid sequence of this oclapeplide?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Graphing the Results from Kinetics Experiments with Enzyme Inhibitors The following kinetic data were obtained for an enzyme in the absence of any inhibitor (1), and in the presence of two different inhibitors (2) and (3) at 5 mM concentration. Assume [ET] is the same in each experiment. Graph these data as Lineweaver-Burk plots and use your graph to find answers to a. and b. a. Determine Vmax and Km for the enzyme. b. Determine the type of inhibition and the K1 for each inhibitor.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of a decapeptide revealed the presence of the following products: The following facts were observed: Neither car boxy peptidase A nor B treatment of the- decapeptide had any effect. Trypsin treatment yielded two tetrapcptides and free Lys. Clostripain treatment yielded a tetrapcptide and a hexapeptidc. Cyanogen bromide treatment yielded an octapeptide and a dipeptide of sequence NP (using the one-letter codes). Chymotrypsin treatment yielded two tripeptides and a telrapeptide. The N-terminal chymotryptic peptide had a net charge of — 1 at neutral pi I and a net charge of —3 al pH 12. One cycle of Ed man degradation gave the PTH derivative What is the ammo acid sequence of this decapeptide?arrow_forward
- Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Draw the Titration Curve for a Weak Acid and Determine its pKa from the Titration Curve When a 0.1 M solution of a weak acid was titrated with base, the following results were obtained: Plot the results of this titration and determine the pK a of the weak acid from your graph.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. A Rule of Thumb for Amino Acid Content in Proteins The simple average molecular weight of the 20 common amino adds is 138, but most biochemists use 110 when estimating the number of amino acids in a protein of known molecular weight. Why do you Suppose this is? (Hint: There are two contributing factors to the answer. One of them will be apparent from a brief consideration of the amino acid compositions of common proteins. See, for example, Figure 5.16 of this text.)arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of ail oligopeptide seven residues long gave The following fads were observed: a. Trypsin treatment had no apparent effect. b. The phenylthiohydantoin released by Lid mini degradation was c. Brief chymotrypsin treatment yielded several products, including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lyi. and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Lys. What is the amino acid sequence of this heptapeptide?arrow_forward
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