Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 9, Problem 12P
Interpretation Introduction
To select:
The peptides that is most likely to acquire an N-terminal myristoyl lipid anchor should be identified.
Introduction:
N-Terminal. In a molecule of the peptide, an amino acid deposit on the one end contains an
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Biochemistry
Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Prob. 4PCh. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...
Ch. 9 - Prob. 11PCh. 9 - Prob. 12PCh. 9 - Answers to all problems are at the end of this...Ch. 9 - Prob. 14PCh. 9 - Prob. 15PCh. 9 - Prob. 16PCh. 9 - Answers to all problems are at the end of this...Ch. 9 - Prob. 18PCh. 9 - Prob. 19PCh. 9 - Prob. 20PCh. 9 - Prob. 21PCh. 9 - Prob. 22PCh. 9 - Prob. 23PCh. 9 - Prob. 24PCh. 9 - Answers to all problems are at the end of this...Ch. 9 - Prob. 26PCh. 9 - Prob. 27PCh. 9 - Prob. 28PCh. 9 - Prob. 29PCh. 9 - Prob. 30PCh. 9 - Prob. 31P
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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. (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 οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Review the mechanisms of the .serine and aspartic proteases, and compare these two mechanisms carefully. Are there steps m die mechanisms that are similar? How are they similar? How are they different? Suggest experiments that could support or refute your hypotheses.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. 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_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. Table 5.4 presents some of the many known mutations in the genes encoding the a- and -globin subunits of hemoglobin. a. Some of these mutations affect subunit interactions between the Subunits. In an examination of the tertiary structure of globin chains, where would you expect to find amino acid changes in mutant globins that affect formation of the hemoglobin 22quaternary structure? b. Other mutations, such as the S form of the-globin chain, increase the tendency of hemoglobin tetramers to polymerize into very large structures. Where might you expect the amino acid substitutions to be in these mutants?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
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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. The Strength of Weak Forces Determines the Environmental Sensitivity of Living Cells Why does the central role of weak forces in biomolecular interactions restrict living systems to a narrow range of environ¬mental conditions? (Section 1.4)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 of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Comparing Membrane Barrel Structures Compare the porin proteins, which have transmembrane pores constructed from -barrels, with the Wza protein, which has a transmembrane pore constructed from a ring of -helices. How many amino acids are required to form the -barrel of a porin? How many would be required to form the same-sized pore from -helices?arrow_forward
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