Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 8, 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.
Understanding Isoprene Structures Refer to Figure 8.13 and draw each of the structures shown and try to identify the isoprene units in each of the molecules. (Note that there may be more than one correct answer for some of these molecules, unless you have the time and facilities to carry out 14C labeling studies with suitable organisms.)
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Biochemistry
Ch. 8 - Answers to all problems are at the end of this...Ch. 8 - Answers to all problems are at the end of this...Ch. 8 - Answers to all problems are at the end of this...Ch. 8 - Answers to all problems are at the end of this...Ch. 8 - Answers to all problems are at the end of this...Ch. 8 - Answers to all problems are at the end of this...Ch. 8 - Answers to all problems are at the end of this...Ch. 8 - Prob. 8PCh. 8 - Answers to all problems are at the end of this...Ch. 8 - Prob. 10P
Ch. 8 - Prob. 11PCh. 8 - Answers to all problems are at the end of this...Ch. 8 - Prob. 13PCh. 8 - Prob. 14PCh. 8 - Prob. 15PCh. 8 - Answers to all problems are at the end of this...Ch. 8 - Prob. 17PCh. 8 - Prob. 18PCh. 8 - Prob. 19PCh. 8 - Prob. 20PCh. 8 - Answers to all problems are at the end of this...Ch. 8 - Answers to all problems are at the end of this...Ch. 8 - 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. 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. Assessing the pH Dependence of Poly-L-Glutamate Structure Poly-L glutamate adopts an tr-helical structure at low pH but becomes a random coil above pH 5. Explain this behavior.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_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. Use examples from the ActiveModel for Human GaleLtin-1 to describe the hydrophobic effect.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 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. Plot the Titration Curve for Bicine and Calculate How to Prepare a pH 7.5 Bicine Buffer Solution Bicine (N, N—bis (2-hydroxyethyl) glycine) is another commonly used buffer in biochemistry labs. The structure of Bicine in its fully protonated form is shown here: Draw the titration curve for Bicine. assuming the pA'a for its free COOH group is 2.3 and the pAa for its tertiary amino group is 8.3. Draw the structure of the fully deprotonated form (completely dissociated form) of bicine. You have available a U.l Msolution of Bicine at its isoelectric point (pH|)T 0.1 M solutions of HCI and NaOH. and ample distilled water. Describe the preparation of 1 L of 0.U4 M Bicine buffer. pH 7.5. What is the concentration of the fully protonated form of Bicine in your final buffer solution?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. 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_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. Calculating [H+] from pH Calculate the following from the pH values given in Table 2.3. [H+] in vinegar [H+] in saliva [H+] in household ammonia [OH-] in milk of magnesia [OH-] in beer [H+] inside a liver cellarrow_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. 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. Writing Dissociation Equations for Amino Acids Write equations fur the ionic dissociations of alanine, glutamate, histidine, lysine, and phenylalanine.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. To fully appreciate the elements of secondary structure in proteins, it is useful to have a practical sense of their structures. On a piece of paper, draw a simple but large zigzag pattern to represent a -strand. Then fill in the structure, drawing the locations of the moms of the chain on this zigzag pattern. Then draw a simple, large coil on a piece of paper to represent an -helix. Then fill in the structure, drawing the backbone atoms in the correction locations along the coil and indicating the locations of the R groups in your drawing.arrow_forward
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