EBK BIOCHEMISTRY
6th Edition
ISBN: 9781337431200
Author: GRISHAM
Publisher: CENGAGE LEARNING - CONSIGNMENT
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Chapter 11, Problem 11P
Answers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book.
Calculating Tms and Separating DNA Molecules That Differ in G:C Content At 0.2 M Na+, the melting temperature of double-stranded DNA is given by the formula, Tm = 69.3 + 0 41 (% G + C). The DNAs from mice and rats have (G + C) contents of 44% and 40%, respectively. Calculate the Tms for these DNAs in 0.2 M NaCl. If samples of these DNAs were inadvertently mixed, how might they be separated from one another?
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Chapter 11 Solutions
EBK BIOCHEMISTRY
Ch. 11 - Answers to all problems are at the end of this...Ch. 11 - Answers to all problems are at the end of this...Ch. 11 - Prob. 3PCh. 11 - Answers to all problems are at the end of this...Ch. 11 - Answers to all problems are at the end of this...Ch. 11 - Answers to all problems are at the end of this...Ch. 11 - Answers to all problems are at the end of this...Ch. 11 - Answers to all problems are at the end of this...Ch. 11 - Prob. 9PCh. 11 - Prob. 10P
Ch. 11 - Answers to all problems are at the end of this...Ch. 11 - Prob. 12PCh. 11 - Prob. 13PCh. 11 - Prob. 14PCh. 11 - Answers to all problems are at the end of this...Ch. 11 - Prob. 16PCh. 11 - Prob. 17PCh. 11 - Prob. 18PCh. 11 - Prob. 19PCh. 11 - Prob. 20PCh. 11 - Prob. 21PCh. 11 - Prob. 22PCh. 11 - Prob. 23P
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- 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
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