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 Length of a Keratin Molecule The central rod domain of a keratin protein is approximately 312 residues in length. What is the length (in A) of the keratin rod domain? If this same peptide segment were a true
To Determine: The length of the keratin rod domain should be determined along with the length of the peptide segment when the same peptide segment were a true a helix. Length of the segment should be determined when the same segment were a ß sheet.
Introduction: One turn of a helix represents
Beta sheet structure can be pictured as a twofold helix with two residues per turn. The distance between residues in the anti-parallel pleated sheet is
Explanation of Solution
The length of the keratin rod domain =
If the segment were a true helix =
If the segment were an antiparallel beta-sheet =
If the segment were a parallel beta-sheet =
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Chapter 6 Solutions
Biochemistry
- 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. Evaluation of -Helices in Proteins The hem agglutinin protein in influenza virus contains a remarkably long -helix, with 53 residues. How long is this -helix (in nm)? How many turns does this helix have? The typical residue in an -helix is involved in two H bonds. How many H bonds are present in this helix?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. 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
- 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. Exploring the Dimensions of the α-Helix and Coiled Coils Imagine that the dimensions of the alpha helix were such that there were exactly 3.5 amino acids per turn instead of 3.6. What would be the consequences for coiled-coil structures?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. Protein Structure Evaluation Based on Gel Filtration Data A new protein of unknown structure has been purified. Gel filtration chromatography reveals that the native protein has a molecular weight of 240,000. Chromatography in the presence of 6 M guanidine hydrochloride yields a single peak corresponding to a protein of Mr 60.000. Chromatography in the presence of 6 M guanidine hydrochloride and 10mM -mercaptoethanol yields peaks for proteins of Mr 34,000 and 26,000. Explain what can be determined about the structure of this protein from these data.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. (Research Problem) Conformational Transitions in Proteins How do proteins accomplish conformational changes? How is it that proteins convert precisely and efficiently from one conformation to another'.’ Recall from Figure 6.54 that any folding/unfolding transition must involve movement across a free-energy landscape, and try to imagine the nature of a conformational transition. Are bonds formed and broken along the way'.' What kinds of bonds and interactions might be involved? Suggest how such conformational transitions might occur. One reference that will be useful in this regard is: Boehr. D.. 2009. During transitions proteins make fleeting bonds. Cell 139: 1049-1051.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. Proteins and nucleic acids are informational macromolecules. What are the two minimal criteria for a linear informational polymer?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. 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_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. Calculation of Phospholipid-to-Protein Ratios The purple patches of the Halobacterium halobium membrane, which contain the protein bacteriorhodopsin, are approximately 75% protein and 25% lipid. If the protein molecular weight is 26,000 and an average phospholipid has a molecular weight of 800. calculate the phospholipid-to-protein mole ratio.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 of Protein-Protein Interactions How do proteins interact? When one protein binds to another, one or both changes conformation. Two hypotheses have been proposed to describe such binding: In the induced fit model, the interaction between a protein and a ligand induces a conformation change (in the protein or ligand) through a step wise process. In the conformational selection model, the unliganded protein (in the absence of the ligand) exists as an ensemble of conformations in a dynamic equilibrium. The binding ligand interacts preferentially with one among many of these conformations and shifts the equilibrium in favor of the selected conformation. Three recent papers shed light on this question: Boehr, D.. and Wright, P. E., 2008. How do proteins interact? Science 320:1429-1430. Gsponer, J.. et al., 200&. A coupled equilibrium shift mechanism in calmodulin-mediated signal transduction. Structure 16:736—'746. Lange, O., et al., 2008. Recognition dynamics up to microseconds revealed from an R DC-derived ubiquitin ensemble in solution. Science 320:1471-1475. Consult these papers and answer the following questions: What proteins were studied in these papers? What techniques were used, and what time scales of protein motion were studied? What were the conclusions of these papers, and how do these results illuminate the choice between induced fit and conformational selection in protein-protein interactions?arrow_forwardAnswers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Superbug infections are becoming more common around the world. Many of these infections arise from the action of -lactamases, of which there are several types with different mechanisms of action. Consult the end-of-chapter reference by von Nussbaum and Schiffer and write detailed mechanisms for the serine -lactamases and metallo- -lactamases.arrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning