FUNDAMENTALS OF BIOCHEMISTRY WPNG 1-SEME
5th Edition
ISBN: 9781119750192
Author: Voet
Publisher: WILEY
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Question
Chapter 27, Problem 22CQ
Summary Introduction
To identify: The normal polypeptide sequence for the given partial mRNA sequence.
Concept introduction: The protein molecules are the essential nutrients of the body. Proteins are synthesized in the ribosomes of the cell. Transcription is the process of the production of mRNA from DNA molecules. mRNA sequences carry the information from one generation to another. Translation is the process of synthesizing protein molecules.
Given: GAUUCCUUUCGUCAGUCCGAGA.
Summary Introduction
To identify: The polypeptide sequence with frameshift for the given partial mRNA sequence.
Concept introduction: The protein molecules are the essential nutrients of the body. Proteins are synthesized in the ribosomes of the cell. Transcription is the process of production of mRNA from the DNA molecules. mRNA sequences carry the information from one generation to another. Translation is the process of synthesizing protein molecules.
Given: GAUUCCUUUCGUCAGUCCGAGA.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
Compare and contrast the structural features of the ion carrier valinomycin with those of achannel former like gramicidin. How does structural information help explain the mechanismby which these molecules conduct ions across membranes?
A typical integral membrane protein has a stretch (or stretches) of ~20 hydrophobic aminoacids that form an α-helix that spans the bilayer (as is found in membrane proteins such asglycophorin A and bacteriorhodopsin). Compare and contrast the molecular and structural
features of gramicidin with a membrane-spanning α-helix. Explain how gramicidin can forman ion channel when a typical membrane-spanning α-helix cannot (eg, glycophorin A).
The titration curve of alanine shows the ionization of two functional groups with pK values of 2.34 and 9.69, corresponding to
the ionization of the carboxyl and the protonated amino groups, respectively. The titration of di-, tri-, and larger oligopeptides of
alanine also shows the ionization of only two functional groups, although the experimental pK values are different. The table
summarizes the trend in pK values.
Amino acid or peptide
Ala
Ala-Ala
pKj
pk₂
2.34
9.69
3.12
8.30
Ala-Ala-Ala
3.39
8.03
Ala-(Ala)-Ala, n ≥ 4
3.42
7.94
Modify the molecules to show the oligopeptide Ala-Ala-Ala. You can modify the molecules by moving, adding,
deleting, or changing atoms, bonds, or charges.
C
Select
c
Draw
Templates
More
H с N 0
S
Cl
H
H
| | ||
H CH3
H
CH,
H CH₂
Complete the statements about the the pK, values of the Ala-Ala-Ala oligopeptide.
The pK₁ value of 3.39 is associated with the
-COO group of Ala-Ala-Ala.
The pK2 value of 8.03 is associated with the -NH
group of Ala-Ala-Ala.
Erase
Q2 Q…
Chapter 27 Solutions
FUNDAMENTALS OF BIOCHEMISTRY WPNG 1-SEME
Ch. 27 - Prob. 1ECh. 27 - Prob. 2ECh. 27 - Prob. 3ECh. 27 - 4. Which amino acids arc specified by codons that...Ch. 27 - 5. In the genetic code used by mitochondria in...Ch. 27 - 6. Some mitochondria use a second codon, in...Ch. 27 - 7. The protein Xpot transports tRNAs out of the...Ch. 27 - 8. The enzyme thiouridylase converts certain tRNA...Ch. 27 - Prob. 9ECh. 27 - 10. Some mutations that do not alter the identity...
Ch. 27 - Prob. 11ECh. 27 - Prob. 12ECh. 27 - Prob. 13ECh. 27 - Prob. 14ECh. 27 - Prob. 15ECh. 27 - Prob. 16ECh. 27 - Prob. 17ECh. 27 - Prob. 18ECh. 27 - 19. Cells can make certain oligopeptides using...Ch. 27 - 20. The peptidyl transferase activity of the...Ch. 27 - 21. One cause of the neurodegeneratise disease...Ch. 27 - Prob. 22CQCh. 27 - 23. A double-stranded fragment of viral DNA, one...Ch. 27 - 24. The sequence of the sense strand of a...Ch. 27 - Prob. 25CQCh. 27 - Prob. 26CQCh. 27 - Prob. 27CQCh. 27 - 28. It has been proposed that residue A2486 is...Ch. 27 - 29. Explain why a minimum of 32 tRNAs are required...Ch. 27 - 30. Under conditions of nutrient starvation,...Ch. 27 - 31. All cells contain an enzyme called...Ch. 27 - Prob. 32CQCh. 27 - Prob. 33CQCh. 27 - Prob. 34CQCh. 27 - Prob. 35CQCh. 27 - Prob. 36CQCh. 27 - Prob. 1MTE
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
- Facts from the bacterium mals and to dept kan apa in a peptide with antidic properties. This peptide complex with the call membrance of other hacterial species, leading in bacterial death The structure of the peptide has been determined from (a) Cmplete acid hydes of the peptide, followed by amino acid analys, yielded quiar anunt of Lan, Om, Pfx, Prxa, and Wall Cmtiti, an amino acid od prosentin pockets but present in some peptides. Com has the tracture H *H,N-CH-CH-CH, -C- COO (b) The weight of the peptide in approximately 1,200 Th (c) The peptide failed to undergo hydrolysis when treated with the Hydrolysis of the carbonyl-terminal residue of a polypeptide une "NH, the year. This call there Pro or the police does not contain a froz (d) Treatment of the peptide with 1-haw-2,4-dicherer (11N1), followed by complete hydrolysis and ched only from and the derivative NO, Н ON NHCHI CH, CH, C coo +NH, (Hint: The 2,4-diphenyl derivative involves the amino group of a side chain rather than the…arrow_forwardElectrophoresis Macmillan Learning Chymotrypsin is a protease with a molecular mass of 25.6 kDa. The figure shows a stained SDS polyacrylamide gel with a single band in lane I and three bands of lower molecular weight in lane 2. Lane I contains a preparation of chymotrypsin and lane 2 contains chymotrypsin pre-treated with performic acid. 1 2 Why does performic acid treatment of chymotrypsin generate three bands in lane 2? ° Chymotrypsin self-digests on the carboxyl-terminal side of phenylalanine, tryptophan, or tyrosine residues. The three peptides are impurities in the original chymotrypsin sample. Performic acid cleaves proteins on the carboxyl-terminal side of lysine and arginine residues. Performic acid cleaves the disulfide bonds holding together the three subunits of chymotrypsin. Correct Answerarrow_forwardExtracts from the bacterium Bacillus brevis contain a peptide with antibiotic properties. This peptide forms complexes with metal ions and seems to disrupt ion transport across the cell membranes of other bacterial species, leading to bacterial death. The structure of the peptide has been determined from a series of observations. (a) Complete acid hydrolysis of the peptide, followed by amino acid analysis, yielded equimolar amounts of Leu, Orn, Phe, Pro, and Val. Orn is ornithine, an amino acid not present in proteins but present in some peptides. Orn has the structure H 'H,N-CH, - CH2 CH2 CH2 - C - COO- NH, (b) The molecular weight of the peptide is approximately 1,200 Da. (c) The peptide failed to undergo hydrolysis when treated with the enzyme carboxypeptidase. This enzyme catalyzes the hydrolysis of the carboxyl-terminal residue of a polypeptide unless the residue is Pro or the peptide does not contain a free carboxyl group. (d) Treatment of the intact peptide with…arrow_forward
- At a pH equal to the isoelectric point (pl) of alanine, the net charge of alanine is zero. Two structures can be drawn that have a net charge of zero, but the predominant form of alanine at its pl is zwitterionic. CH3 H,N CH3 ** H¸N-C H Zwitterionic H Uncharged OH Select statements that explain why alanine is predominantly zwitterionic at its pl. pk of alanine's amino group is more than its pl. pk of alanine's carboxyl group is more than its pl. PK of alanine's carboxyl group is less than its pl. pk of alanine's amino group is less than its pl. Correct Answer What fraction of alanine is in the completely uncharged form at its pl? 1 in 2.2 × 107 1 in 1.6 × 10² 1 in 4680 1 in 9460arrow_forwardHow does a voltage-gated sodium channel work? Specifically, how and why does a change in voltage trigger their opening? Please be detailedarrow_forwardWhen sodium ions enter a neuron during depolarization, they trigger the opening of additional voltage-gated sodium channels nearby, creating a positive feedback loop where the influx of sodium ions further depolarizes the membrane, causing even more sodium channels to open and allowing more sodium ions to enter the cell, thus sustaining the depolarization process until the action potential peaks. But how and why exactly does the influx of sodium ions trigger more sodium channels to let in more sodium? Please explainarrow_forward
- Draw the predominant form of glutamic acid at pH = 8.4. The pKa of the side chain is 4.1. Include proper stereochemistry. HO H2N OH pH = 8.4arrow_forwardHow would I draw this?arrow_forwardCalculate the standard change in Gibbs free energy, AGrxn, for the given reaction at 25.0 °C. Consult the table of thermodynamic properties for standard Gibbs free energy of formation values. NH,Cl(s) →NH; (aq) + C1 (aq) AGrxn -7.67 Correct Answer Determine the concentration of NH+ (aq) if the change in Gibbs free energy, AGrxn, for the reaction is -9.27 kJ/mol. 6.49 [NH+] Incorrect Answer kJ/mol Marrow_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