Biochemistry: Concepts and Connections
1st Edition
ISBN: 9780321839923
Author: Dean R. Appling, Spencer J. Anthony-Cahill, Christopher K. Mathews
Publisher: PEARSON
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Chapter 4, Problem 8P
Refer to Figure 4.15, which presents the Meselson-Stahi experiment. DNA molecules can be denatured by high pH, as well as by heat. Suppose that the CsCl gradient centrifugations were run at pH 12, conditions under which DNA strands separate. Sketch the gradient profiles expected for each of the four samples depicted in the figure.
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Chapter 4 Solutions
Biochemistry: Concepts and Connections
Ch. 4 - Prob. 1PCh. 4 - What is the difference between a nucleoside...Ch. 4 - pppApCpCpupApGpApu-OH a. Using the straight-chain...Ch. 4 - Shown is a representation of a molecule being...Ch. 4 - Base analysis of DNA from maize (com) shows it to...Ch. 4 - Using the pKa data in Table 4.1 and the...Ch. 4 - For some DNAs, it is possible to separate the two...Ch. 4 - Refer to Figure 4.15, which presents the...Ch. 4 - Suppose that you centrifuged a transfer RNA...Ch. 4 - Predict the structure of a cruciform that could be...
Ch. 4 - DNA from a newly discovered virus was purified,...Ch. 4 - Would you expect Neurospora crassa DNA to have a...Ch. 4 - A circular double-stranded DNA molecule contains...Ch. 4 - The gel electrophoresis pattern in Figure 4.23 was...Ch. 4 - 15. DNA polymerase requires both a template, to be...Ch. 4 - Prob. 16P
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- 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.arrow_forwardA 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 AKGEDarrow_forwardMelting 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_forward
- Select 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_forwardWhich is a homotropic positive effector of aspartate transcarbamoylase (ATCase)? oxygen CTP aspartate ATParrow_forward
- The 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_forwardThe 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_forward
- Which 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_forwardSelect 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_forward
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