Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 15, Problem 16P
Interpretation Introduction
To illustrate:
The two monomer conformations, tetramer and trimer showing how tetramer is stable.
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Chapter 15 Solutions
Biochemistry
Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Prob. 5PCh. 15 - Prob. 6PCh. 15 - Prob. 7PCh. 15 - Prob. 8PCh. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...
Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Answers to all problems are at the end of this...Ch. 15 - Prob. 14PCh. 15 - Prob. 15PCh. 15 - Prob. 16PCh. 15 - Prob. 17PCh. 15 - Prob. 18PCh. 15 - Prob. 19PCh. 15 - Prob. 20PCh. 15 - Prob. 21PCh. 15 - Prob. 22PCh. 15 - Prob. 23PCh. 15 - Prob. 24P
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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 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 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_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. Examine the ActiveModle for N-myristoylt ranjsferase and explain the mechanism of N-myristolation.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. 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_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. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of an oligopeptide containing nine residues revealed the presence of the following amino adds: Arg Cys Gly Leu Met Pro Tyr Val The following was found: Carboxypeptidase A treatment yielded no free amino add. Edman analysis of the intact oligopeptide released c. Neither trypsin nor ehymotrypsin treatment of the nonapeptide released smaller fragments. However, combined trypsin and chymotrypsin treatment liberated free Arg. CNBr treatment of the eight-residue fragment left after combined trypsin and chymotrypsin action yielded a six-residue fragment containing Cys* Gly. Pro, Tyr, and Val and a dipeptide. Treatment of the six-residue fragment with -mercaptoethanol yielded two tripeptidcs. Brief Edman analysis of the tripeplide mixture yielded only Ρ�Ή-Cys. (The sequence of each tripeptide, as read from the N-terminal end, is alphabetical if the one-lelter designation for amino acids is used.) What is the amino acid sequence of this nonapeptide?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. 13. Determining Tyrosine Content of an Unknown Protein A previously unknown protein has been isolated in your laboratory. Others in your lab have determined that the protein sequence contains 172 amine acids. They have also determined that this protein has ne tryptophan and no phenylalanine. You have been asked to determine the possible tyrosine content of this protein. You know from your Study of this chapter that there is a relatively easy way to do this. You prepare a pure 50 mM solution of the protein, and you place it in a sample cell with a 1-em path length, and yen measure the absorbance of this sample at 280 nm in a U V-visible spectrophotometer. The absorbance of the solution is 0.372. Are there tyrosines in this protein? How many? (Hint: You will need to use Beer's law, which is described in any good general chemistry or physical chemistry textbook. You will also find it useful le know that the units of molar absorptivity are M-1cm-1.)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-DNA Interactions Gerie expression is controlled through the interaction of proteins with specific nucleotide sequences in double stranded DNA. List the kinds of noncovalent interactions that might take place between a protein and DNA. How do you suppose a particular protein might specifically interact with a particular nucleotide sequence in DNA'.’ That is. how might proteins recognize specific base sequences within the double 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. 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
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