Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Textbook Question
Chapter 6, Problem 3P
A schematic structure of the subunit of hemerythrin (an oxygen-binding protein from invertebrate animals) is shown to the right.
a. It has been found that in some of the a-helical regions of hemerythrin, about every third or fourth amino acid residue is a hydrophobic one. Suggest a structural reason for this finding.
b. What would be the effect of a mutation that placed a proline residue at point A in the structure?
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Check out a sample textbook solutionStudents have asked these similar questions
i. A schematic structure of the subunit of hemerythrin (an oxygen-binding
protein from invertebrate animals) is shown to the right.
(a) It has been found that in some of the a-helical regions of hemerythrin,
about every third or fourth amino acid residue is a hydrophobic one.
Suggest a structural reason for this finding.
(b) What would be the effect of a mutation that placed a proline residue at
point A in the structure?
In the molecule of oligomeric protein there are
19 lysine residues. 12 of them may be easily
acetylated with anhydrides of dicarbon acids
(it react with NH2-groups). The acetylation of
extra two residues of lysine will dissociate the
protein to the subunits. The rest 5 lysine
residues may be modified only after
denaturation of the protein. Suggest, how
many lysine residues are:
a) on a surface of protein globule;
b) inside globule:
c) in a site which is responsible for the contact
within subunits
A protein hypothetically consists of two polypeptide chains with the given sequences in the picture.
Based on the said sequences,
a. Do you think it is possible that interchain disulfide bonds is present in the protein? Explain.
b. Do you think it is possible that intrachain disulfide bonds is present in the protein? Explain.
Chapter 6 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 6 - Prob. 1PCh. 6 - Bovine pancreatic trypsin inhibitor (BPTI; Figure...Ch. 6 - A schematic structure of the subunit of...Ch. 6 - In the protein adenylate kinase, the C-terminal...Ch. 6 - Give two reasons to explain why a proline residue...Ch. 6 - Consider a small protein containing 101 amino acid...Ch. 6 - a. Based on a more conservative answer to Problem...Ch. 6 - The following sequence is part of a globular...Ch. 6 - a. A protein is found to be a tetramer of...Ch. 6 - Under physiological conditions, the protein...
Ch. 6 - Theoretical and experimental measurements show...Ch. 6 - The peptide hormone vasopressin is used in the...Ch. 6 - A protein gives under conditions of buffer...Ch. 6 - A protein gives a single band on SDS get...Ch. 6 - It has been postulated that the normal...Ch. 6 - Below are shown two views of the backbone...Ch. 6 - Do you expect a Pro Gly mutation in a...Ch. 6 - Rank the following in terms of predicted rates...Ch. 6 - Shown below are two cartoon views of the small...Ch. 6 - Prob. 20PCh. 6 - In most cases, mutations in the core of protein...Ch. 6 - A Leu Ala mutation at a site buried the core of...Ch. 6 - Disulfide bonds have been shown to stabilize...Ch. 6 - Cartoon renderings of the proteins Top 7 and adaH2...
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- To better understand the effects of palmitoylation on protein X, researchers want to chemically attach a palmitic acid at a specific position in this protein. The researchers first try to feed cells with palmitic acid or an amino acid with a C16 side chain. Neither of the initial experiments is successful in helping the researchers learn more about the biological role of palmitoylated protein X. Why? Suggest a strategy to specifically incorporate a palmitoylation site into protein X.arrow_forwardwhat is the c-terminal AA residue? use one-letter code for amino acidarrow_forwardFor the peptide Ala-Cys-His-Ile-Leu-Asp a. Write the single letter code for the amino acid residues b. What is the charge of the peptide at pH 7.0. Assign the following pKa values: 3,4,6,8,9 c. What is the pI of the peptidearrow_forward
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