Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 6, Problem 11P
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 Η-Bond Formation in Proteins Which amino acids would be capable of forming H bonds with a lysine residue 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. 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. 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. 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_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. 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. (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_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. (Historical Context) The Third Person of the -Helix Publication Who was Herman Branson? What was his role in the elucidation of the structure of the or-helix'.' Did he receive sufficient credit and recognition for his contributions? And how did the rest of his career unfold? Do a Google search on Herman Branson to learn about his life, and read the article by David Eisenberg under Further Reading. You may also wish to examine the original paper by Pauling, Corey, and Branson, as well as the following Web site: http://www.pirns. org/sitelmisclclassicsl..shtml Pauling, L., Corey, R. B., and Branson, H. R., 1951. The structure of proteins: two hydrogen-bonded helical configurations of the polypeptide chain. Proceedings of the National Academy of Sciences, USA 37:235-240.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. Determining the Systematic Name for a Trisaccharide Give the systematic name for it stachyose.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 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. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of a decapeptide revealed the presence of the following products: The following facts were observed: Neither car boxy peptidase A nor B treatment of the- decapeptide had any effect. Trypsin treatment yielded two tetrapcptides and free Lys. Clostripain treatment yielded a tetrapcptide and a hexapeptidc. Cyanogen bromide treatment yielded an octapeptide and a dipeptide of sequence NP (using the one-letter codes). Chymotrypsin treatment yielded two tripeptides and a telrapeptide. The N-terminal chymotryptic peptide had a net charge of — 1 at neutral pi I and a net charge of —3 al pH 12. One cycle of Ed man degradation gave the PTH derivative What is the ammo acid sequence of this decapeptide?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_forward
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