Fundamentals of Biochemistry: Life at the Molecular Level
5th Edition
ISBN: 9781118918401
Author: Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher: WILEY
expand_more
expand_more
format_list_bulleted
Concept explainers
Question
Chapter 26, Problem 16E
Summary Introduction
To explain: The biological function of linking of 5ʹ end of regulatory RNAs to 3ʹ-OH group of adenosine residue of NAD+ and how the activity of a modified RNA might reflect the cell’s overall
Introduction: Bacterial RNA polymerases initiate transcription with the adenosine residue of NAD+. Bacterial regulatory RNAs are a group of heterogenous molecules such as riboswitches. They act to modulate various physiological responses.
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solutionStudents have asked these similar questions
Geranylgeranyl pyrophosphate 5 is converted by general acid-base catalysis to 6, and then to the natural product 7. For clarity only limited atom numbers are shown, but the main chain carbons are numbered 1 to 16, and the off-chain methyl substituents are numbered 17-20.
A. Based on what you specified in A, use curly arrows on the drawing above to convert 5 to 6, and 6 to 7. Invoke general acids and general bases as needed, and draw in hydrogens as necessary .
B. On the structure of 7, write in the atom numbers for the carbons marked with an asterisk
α-Pinene (4) is synthesized enzymatically from nerol pyrophosphate 1. Drawn an arrow-pushing mechanism from 1 to 2 to 3 to 4; add explicit hydrogens to clarify, if needed.
A reverse phase column chromatography separates proteins according to their polarity. Which pentapeptide will be eluted FIRST when chromatographed at pH 7 using a reverse phase column such as a C-18 column?
Peptide Sequence (from N-terminal to C-terminal)
AKGED
GAAVF
ALLLI
MCYAG
GAAVF
MCYAG
ALLLI
AKGED
Chapter 26 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 26 - Prob. 1ECh. 26 - 2. The bacterial enzyme polynucleotide...Ch. 26 - Prob. 3ECh. 26 - Prob. 4ECh. 26 - Prob. 5ECh. 26 - Prob. 6ECh. 26 - Prob. 7ECh. 26 - Prob. 8ECh. 26 - Prob. 9ECh. 26 - 10. Certain E. coli bacteriophages encode a...
Ch. 26 - Prob. 11ECh. 26 - Prob. 12ECh. 26 - 13. Compare DNA polymerase, RNA polymerase, poly...Ch. 26 - Prob. 14ECh. 26 - Prob. 15ECh. 26 - Prob. 16ECh. 26 - Prob. 17ECh. 26 - Prob. 18ECh. 26 - Prob. 19ECh. 26 - Prob. 20ECh. 26 - Prob. 21ECh. 26 - Prob. 22ECh. 26 - Prob. 23CQCh. 26 - Prob. 24CQCh. 26 - Prob. 25CQCh. 26 - Prob. 26CQCh. 26 - Prob. 27CQCh. 26 - Prob. 28CQCh. 26 - Prob. 29CQCh. 26 - Prob. 30CQCh. 26 - 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
- Melting of three DNA samples with varying lengths was monitored by increase of ultraviolet light absorbance at 260 nm. Which is the shortest DNA? A B Carrow_forwardSelect the CORRECT description of the peptide bond. The peptide bond can freely rotate around the peptide bond. The peptide bond is non-polar, hydrophobic and does not have a dipole. The peptide bond is most stable in the cis configuration. The peptide bond is rigid and planar. The peptide bond has a mix of single and double bond characters. The peptide bond is most stable in the trans configuration.arrow_forwardBelow is a fractional saturation curve for O2 binding to adult hemoglobin. Assume that curve Y represents a system at pH 7.4 and with a normal physiological level of 2,3-BPG. Curve Z represents a system that ___________________ Curve Z: is at pH 7.4 with a higher than normal physiological level of 2,3-BPG. is at pH 7.4 with a normal physiological level of 2,3-BPG but with a decreased level of CO2. has a higher pH with a normal physiological level of 2,3-BPG. has a higher pH with a lower than physiological level of 2,3-BPG.arrow_forward
- Which is a homotropic positive effector of aspartate transcarbamoylase (ATCase)? oxygen CTP aspartate ATParrow_forwardThe reaction scheme shows the mechanism of chymotrypsin-catalyzed peptide hydrolysis. Select ALL CORRECT statements regarding the chymotrypsin mechanism. Serine is the nucleophile in the step 3. Histidine is a general base in the step 2. Carbonyl carbon is the electrophile in the step 3. Histidine is a general acid in the step 4. Carbonyl carbon is the nucleophile in the step 3. This is an example of covalent catalysis. Aspartate is the electrophile in the step 3. Histidine is the nucleophile in the step 3.arrow_forwardThe following shows a protein with mostly beta sheet secondary structures. Which force stabilizes the beta sheet secondary structure of proteins? hydrophobic interactions between nonpolar amino acid side chains within the protein. electrostatic interactions between lysine and aspartic acid residues within the protein. hydrogen bonding between hydrogen bond donors and hydrogen bond acceptors of the peptide backbone. covalent disulfide linkages between cysteine residues within the protein.arrow_forward
- The Lineweaver-Burk plot was obtained when enzyme inhibition study was done in the absence and presence of 0.50 mM inhibitor. Answer the following questions using correct units and significant figures: (a) What is the mode of inhibition, competitive, uncompetitive, mixed, or noncompetitive? Explain your answer. (b) What can you say about the finding site for the inhibitor in relation to the active site of the enzyme? Explain your answer. (c) Calculate the Km and Vmax in the absence of inhibitor. (d) Calculate the Km and Vmax in the presence of 0.50 mM inhibitor. (e) Calculate the KI of the inhibitor using the given equations for reversible inhibition. Which has a higher affinity, the substrate or the inhibitor? How can you tell?arrow_forwardWhich peptide sequence is most likely to be found in the interior portion of a water-soluble globular protein? GGDGEMG DSKSTEG GAIVLWL IVAKSLIarrow_forwardThe following shows a reaction coordinate diagram. Choose a CORRECT statement explaining the diagram. The size of C decreases in the presence of an enzyme. B indicates the activation energy of the reaction in the presence of an enzyme. C indicates the activation energy of the reaction in the presence of an enzyme. A is related to the equilibrium constant of the reaction in the absence of an enzyme.arrow_forward
- Select ALL correct statements regarding myoglobin and hemoglobin. Statements: Myoglobin has a higher affinity for oxygen than hemoglobin does. Both myoglobin and hemoglobin contain mostly alpha-helical structures. Myoglobin has one binding site for 2,3-BPG. Hemoglobin is a tetramer, each of which binds one heme group. In both myoglobin and hemoglobin, iron ions (Fe2+) bind directly to oxygen. Myoglobin is a tetrameric protein. Hemoglobin exhibits cooperative binding with oxygen. Myoglobin does not. Hydrogen ion, carbon dioxide, and 2,3-BPG are negative allosteric effectors of oxygen binding to hemoglobin. Myoglobin has a lower P50 for oxygen than hemoglobin does. Hemoglobin has a higher affinity for oxygen than myoglobin does. Both myoglobin and hemoglobin exhibit cooperative binding to oxygen.arrow_forwardAn enzyme is found to have maximum activity in a pH range of 6 to 8. It is inactive below pH 3. It is also found that glutamate and serine residues are present at the active site. The mutations of these residues show the following results. Select ALL statements that are consistent with the experimental results. When serine is mutated to alanine, the mutant enzyme is fully active with maximum activity at pH 6 to 8. When glutamate is mutated to alanine, the mutant enzyme is inactive at all pH. The pKa of the side chain of glutamate is 4.25. Glutamate is required for catalysis at pH 6 to 8. Serine is not required for catalysis at pH 6 to 8. Glutamate must be protonated for catalysis at pH 6 to 8. Glutamate must be deprotonated for catalysis at pH 6 to 8. Both serine and glutamate are required for catalysis at pH 6 to 8.arrow_forwardIn the Anfinsen experiment with the denaturation and renaturation of RNaseA, denaturant and reductant were added to RNaseA to produce a denatured structure. In this denaturation experiment, urea was used as denaturant and beta-mercaptoethanol was used as reductant. Then both urea and beta-mercaptoethanol were slowly removed. What will be the result of this experiment? Answers: The resulting protein will be fully active. The resulting protein will not contain any disulfide linkages. The resulting protein will not have the enzyme activity. The resulting protein will not have the native structure.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. FreemanLehninger Principles of BiochemistryBiochemistryISBN:9781464126116Author:David L. Nelson, Michael M. CoxPublisher:W. H. FreemanFundamentals 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 LearningBiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningFundamentals 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