Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 6, Problem 3P
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 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.
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Chapter 6 Solutions
Biochemistry
Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...
Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - Answers to all problems are at the end of this...Ch. 6 - 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. Interpreting Kinetics Experiments from Graphical Patterns The following graphical patterns obtained from kinetic experiments have several possible interpretations depending on the nature of the experiment and the variables being plotted. Give at least two possibilities for each.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. 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_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. 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. 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_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 pH in Amino Acid Solutions II (Integrates with Chapter 2.) Calculate the pH at which the -amino group of lysine is 20% dissociated.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. Consider a protein that can exist in two forms: folded and unfolded. Calculate the free energy difference at 298 k. between a state in which SU% of the protein is folded and a state in which 80%of the protein is unfolded.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. Use examples from the ActiveModel for Human GaleLtin-1 to describe the hydrophobic effect.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 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. 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. (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
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