Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 9, Problem 21P
Interpretation Introduction
Interpretation:
The affect of hydrophobic environment on the dissociation behavior of the side chains of lysine and arginine residues in a protein is to be stated. The reason corresponding to this dissociation behavior is to be stated.
Concept introduction:
Amino acid is a compound that is composed of
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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. The Role of Proline Residues in -Turns Pro is the amino acid least commonly found in «-helices but most commonly found in -turns. Discuss the reasons for 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. Understanding the Role of Gly Residues In Protein Secondary and Tertiary Structure It is often observed that Gly residues are conserved in proteins to a greater degree than other amino acids. From what you have learned in this chapter, suggest a reason for this observation.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 Concentrations of Species in Amino Acid Solutions (Integrates with Chapter 2.) Calculate the concentrations of all ionic species in a 0.25 M solution of histidine at pH 2, pH 6.4, and pH 9.3.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) 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_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 Roles of Weak Forces Between Amino Acids in Proteins Discuss the potential contributions to hydrophobic and van der Waals interactions and ionic and hydrogen bonds for the side chains of Asp, Leu, Tyr and His in a protein.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. Assessing the Range of and Angles in Proteins Choose any three regions in the Ramachandran plot and discuss the likelihood of observing that combination of and in a peptide or protein. Defend your answer using suitable molecular models of a peptide.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 dissociation constant for a particular protein dimer is 1 micromolar. Calculate the free energy difference for the monomer-to-dimer transition.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. (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. 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. Proteins and nucleic acids are informational macromolecules. What are the two minimal criteria for a linear informational polymer?arrow_forward
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