Biochemistry: Concepts and Connections (2nd Edition)
2nd Edition
ISBN: 9780134641621
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 5, Problem 12P
a. Write a possible sequence for an mRNA segment coding for apamine.
b. Do you think apamine is synthesized in the form shown in Problem 11, or is it more likely a product of proteolytic cleavage of a larger peptide? Explain.
11. Apamine is a small protein toxin present in the venom of the honeybee. It has the sequence
CNCKAPETALCARRCQQH
a. If apamine does not react with iodoacetate (see Tools of Biochemistry 5B), then how many disulfide bonds are present?
b. If trypsin cleavage gave two peptides, then where is(are) the S-S bond(s)?
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
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:
%
%
Kindly refer to the photo. Thank you
The following amino acids that are often found inside globulin molecules are ()
A, Tyr B, Phe C, Asn D, Glu
True of false
1. In the de novo synthesis of purine nucleotides and pyrimidine nucleotides, base rings are first
synthesized and then corresponding nucleotides are formed with phosphoribose. ()
2. Transcription is the process of transferring genetic information from DNA to RNA. DNA is
synthesized under the catalysis of RNA polymerase, and the direction of synthesis is from the 5
'end to the 3' end. ()
3. The change of protein conformation is caused by the breaking of covalent bonds within the
molecule. ()
4. In very high and very low pH solutions, amino acids exist mainly in non-ionic form. ()
5. The active center of an enzyme usually consists of several amino acid residues adjacent to each
other in the primary structure. ()
Chapter 5 Solutions
Biochemistry: Concepts and Connections (2nd Edition)
Ch. 5 - Prob. 1PCh. 5 - Draw the structure of the peptide DTLH, showing...Ch. 5 - Prob. 3PCh. 5 - Prob. 4PCh. 5 - Prob. 5PCh. 5 - Prob. 6PCh. 5 - Prob. 7PCh. 5 - Given the following peptide SEPIMAPVEYPK a....Ch. 5 - A mutant form of polypeptide hormone angiotensin...Ch. 5 - Prob. 10P
Ch. 5 - Prob. 11PCh. 5 - a. Write a possible sequence for an mRNA segment...Ch. 5 - 13. Assume the following portion of an mRNA Find a...Ch. 5 - Prob. 14PCh. 5 - Prob. 15PCh. 5 - Prob. 16PCh. 5 - Prob. 17PCh. 5 - Prob. 18PCh. 5 - You are a summer intern in a clinical hematology...Ch. 5 - Prob. 20PCh. 5 - Despite the fact that many peptides have critical...Ch. 5 - Based on the information in Figure 5.17, which...Ch. 5 - If you want to purify a DNA-binding protein from a...
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biochemistry and related others by exploring similar questions and additional content below.Similar questions
- Some types of tumors express cell-surface receptors that are specific for unique peptide sequences. Development of modified peptides that target cancerous cells specifically is an area of active research. One peptide that has been studied extensively is luteinizing hormone-releasing hormone. A portion of the peptide sequence is: HWSYKLRPG. a. Of the nine amino acid sidechains in HWSYKLRPG, how many carry a positive charge at pH 4? at pH 7.4? at pH 11? b. What is the net charge on the peptide HWSYKLRPG at pH 7? c. (optional) For extra practice, draw the structure of HWSYKLRPG in its predominant form at pH 7.4.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_forwardBriefly describe each of the following possible posttranslational protein modifications. Give an example of each. Cross-linkage glycosylation and phosphorylation cleavage assembly into polymeric proteins (> 1 polypeptide)arrow_forward
- Shown to the right is a cartoon image of ETC Complex I from Y. lipolytica. A group of authors studied this wild type Complex I and also a version where the arginine at position 121 in the chain 3 subunit was mutated to a methionine (R121M). Part of chain 3 subunit contains the peptide sequence SMITH a. Draw the titration curve for the SMITH peptide. Mark all pKa’s and the pI on your curve. For the SMITH peptide at physiological pH, explain what types of interactions you believe the side chains are or are not able to participate in.arrow_forwardIf the following truncated peptide represents the active domain of the COVID19’s S-protein N-terminal ----Leu-Leu-Gly-Cys-Ile-Glu-Ser-Thr-Cys-Ala ------ C-terminal a) state the RNA sequence of this peptide given that Leu is the first amino acid b) show a point mutation using the RNA sequence & explain how it results in silent mutation effect c) show a deletion mutation using the RNA sequence & explain the consequence(s)arrow_forwardRemembering that the wobble base of the tRNA is the5′ base of the anticodon:a. In human tRNAs, what are the sequences of allpossible anticodons that were originally transcribedwith A in the wobble position? (Assume this A isalways modified to I.)b. In human tRNAs, what are the sequences of allpossible anticodons that were originally transcribedwith U in the wobble position? (Note: Any singletype of tRNA with a U at the wobble position canbe modified only in a single way.)c. How might the wobble Us in each of the anticodonsin (b) be modified and still be consistent with thegenetic code?d. What is the theoretical minimal number ofdifferent tRNA genes that must exist in thehuman genome? (Assume that xo5U pairs with A,G, or U only.)arrow_forward
- . 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.arrow_forwarda. A single mutation in the riboswitch’s sequence changes the ligand binding specificity from guanine toadenine. Predict what single mutation could be made in the guanine-responsive riboswitch sequenceto convert it to an adenine-responsive riboswitch. Justify your answer b. Could a DNA molecule with the same nucleotide sequence as the guanine-responsive riboswitch bindguanine in a similar manner as the RNA-based molecule? Explainarrow_forward28. a. Can a tRNA exist that has the anticodon sequence 5' IAA? If so, which amino acid would it carry? b. Answer the same question for the anticodon sequence 5' xm³s²UAA. 29. For parts (a) and (b) of Problem 28, consider the DNA sequences of the genes encoding the tRNAs. (Assume both tRNAs exist even if that is not true.) What is the sequence of the RNA-like strand of each tRNA gene that corresponds to the tRNA's anticodon? What is the sequence of the template strand of each gene for these same three nucleotides? Be sure to indicate polarities.arrow_forward
- what is the c-terminal AA residue? use one-letter code for amino acidarrow_forwardThe first 32 amino acids from the N terminus of the protein bovine angiogenin were determined by Edman degradation and have the sequence:AQDDYRYIHFLTQHYDAKPKGRNDEYCFNMMK(a) Identify the sites of cleavage during trypsin-catalyzed hydrolysis of this protein.(b) What are the cleavage sites using chymotrypsin?arrow_forwardOrnithine is structurally similar to lysine except ornithine’s side chain is one methylene group shorter than that of lysine. Attempts to chemically synthesize and isolate ornithinyl-tRNA proved unsuccessful. Propose a mechanistic explanation. (Hint: Six-membered rings are more stable than sevenmembered rings.)arrow_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
BiochemistryBiochemistryISBN:9781319114671Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.Publisher:W. H. Freeman
Lehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...BiochemistryISBN:9781118918401Author:Donald Voet, Judith G. Voet, Charlotte W. PrattPublisher:WILEY
BiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning
BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...BiochemistryISBN:9780134015187Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. PetersonPublisher:PEARSON
Biochemistry
Biochemistry
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:W. H. Freeman
Lehninger Principles of Biochemistry
Biochemistry
ISBN:9781464126116
Author:David L. Nelson, Michael M. Cox
Publisher:W. H. Freeman
Fundamentals of Biochemistry: Life at the Molecul...
Biochemistry
ISBN:9781118918401
Author:Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher:WILEY
Biochemistry
Biochemistry
ISBN:9781305961135
Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal
Publisher:Cengage Learning
Biochemistry
Biochemistry
ISBN:9781305577206
Author:Reginald H. Garrett, Charles M. Grisham
Publisher:Cengage Learning
Fundamentals of General, Organic, and Biological ...
Biochemistry
ISBN:9780134015187
Author:John E. McMurry, David S. Ballantine, Carl A. Hoeger, Virginia E. Peterson
Publisher:PEARSON
QCE Biology: Introduction to Gene Expression; Author: Atomi;https://www.youtube.com/watch?v=a7hydUtCIJk;License: Standard YouTube License, CC-BY