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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Chapter 6, Problem 4P
In the protein adenylate kinase, the C-terminal region has the sequence
Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-
The hydrophobic residues in this sequence are presented in boldface type. Suggest a possible reason for the periodicity in their spacing.
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In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-Ser-Gln-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys-The hydrophobic residues in this sequence are presented in boldface type.Suggest a possible reason for the periodicity in their spacing.
. In the protein adenylate kinase, the C-terminal region is a-helical,
with the sequence
Val-Asp-Asp-Val-Phe-Ser-Gin-Val-Cys-Thr-His-Leu-Asp-
Thr-Leu-Lys-
The hydrophobic residues in this sequence are presented in boldface
type. Suggest a possible reason for the periodicity in their spacing.
In the protein adenylate kinase, the C-terminal region has the sequence Val-Asp-Asp-Val-Phe-
Ser-Gin-Val-Cys-Thr-His-Leu-Asp-Thr-Leu-Lys The hydrophobic residues in this sequence are
presented in boldface type. Use helix wheel to demonstrate this peptide is an amphipathic
helix.
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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- Treatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide. I don't understand how the order of amino acids in Step 2 was arranged. Please explain. Thank you.arrow_forwardTreatment of a polypeptide by 2-mercaptoethanol yields two polypeptides that have the following amino acid sequences: Ala-Phe-Cys-Met-Tyr-Cys-Leu-Trp-Cys-Asn Val-Cys-Trp-Val-Ile-Phe-Gly-Cys-Lys Chymotrypsin-catalyzed hydrolysis of the intact polypeptide yields polypeptide fragments with the following amino acid compositions: (Ala, Phe) (Asn, Cys2, Met,Tyr) (Cys, Gly, Lys) (Cys2, Leu,Trp2,Val) (Ile, Phe,Val) Indicate the positions of the disulfide bonds in the original polypeptide.arrow_forwardSubjecting this peptide to trypsin would result in L-M-F-V-W-E-Q-A-P-S-P O A. Lys and Met-Phe-Val-Trp-Glu-Gln-Arg and Pro-Ser-Pro OB, Leu-Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro Leu and Met-Phe-Val-Trp-Glu-Gln-Arg-Pro-Ser-Pro OC. Op. Lys and Met-Phe-Val-Trp-Glu-Gln-Ala-Pro-Ser-Pro Leu and Met-Phe-Val-Trp-Glu-Gin-Arg-Pro-Ser-Pro OE.arrow_forward
- Members of the integrin family are the major cell surface receptors for many ECM proteins such as fibronectin. In experimental studies, single integrin heterodimers have been found to assume more than one structural conformation. Describe the relationship between integrin structures and their activities.arrow_forwardA binding curve for the binding of the amino acid tryptophan to the protein called TxtE is shown below. Estimate the association equilibrium constant (Ka; in units of M-1) for Trp binding to TxtE.arrow_forwardMany blood clotting proteins undergo a post-translational modification in which specific glutamic acid residues (Glu) in the protein are converted to gamma-carboxyglutamic acid residues (Gla). See reaction scheme below. An example is the blood clotting protein Factor IX, which has 12 Glu in its N-terminus converted to Gla. This modification gives Factor IX the ability to bind calcium and phospholipid membranes. Bacteria do not have the enzyme required to convert Glu to Gla and therefore Factor IX proteins expressed in bacteria would not have the proper modifications. How might you engineer the translational apparatus of a bacterial cell line so that it produces Factor IX with Gla in the appropriate positions. How would you ensure that only the 12 Glu in Factor IX that are normally converted to Gla and not just all Glu (Limit 5-6 senetnces)?arrow_forward
- A peptide with the primary structure Lys-Arg-Pro-Leu-Ile-Asp-Gly-Ala must be synthesized by the methods developed by Merrifield. Calculate the percentage of the peptides synthesized that will be full length and have the correct sequence if the addition of each amino acid residue is 96% efficient. Do the calculation a second time but assume a 99% efficiency for each cycle. full-length peptides with the correct sequence if 96% efficient: full-length peptides with the correct sequence if 99% efficient: % %arrow_forwardprovide examples of the levels of protein structure for mevalonate kinase (2HFU) provide the levels of protein structure (primary, secondary, tertiary, etc.) for mevalonate kinase (2HFU)arrow_forwardSome protein kinases are inactive unless they are phosphorylated on key serine or threonine residues. In some cases, active enzymes can be generated by mutating these serine or threonine residues to aspartate. Explain.arrow_forward
- Crystal structures exist for three neurokinin-1 (NK1) ligand complexes with the following pdb codes (6hll, 6hlo, 6hlp) For each of the three crystal structures identify four amino acids in the NK1 binding site that contact the ligand indicating both the residue type in three letter code and the residue number. One of the chose amino acids should form a hydrogen binding interaction to the ligand, state which functional group the amino acid utilises in each casearrow_forwardThe peptide Leu-Cys-Arg-Ser-Gln-Met is subjected to Edman degradation. After the first cycle of this process, the products that are generated are: O PTH-Leu, PTH Cys, PTH-Arg. PTH-Ser, PTH-GIn, and PTH-Met O PTH-Leu-Cys-Arg-Ser-Gin-Met O PTH-Met and Leu-Cys-Arg-Ser-Gin-Met O PTH-Leu-Cys and PTH-Arg-Ser-Gin-Met O PTH-Leu and Cys-Arg-Ser-Gln-Metarrow_forwardSome protein kinases are inactive unless they are phosphorylated on key serine or threonine residues. In some cases, active enzymes can be generated by mutating these serine or threonine residues to glutamate. Explain. What could you predict about a mutant generated replacing the serine or threonine with alanine.arrow_forward
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