Fundamentals of Biochemistry: Life at the Molecular Level
5th Edition
ISBN: 9781118918401
Author: Donald Voet, Judith G. Voet, Charlotte W. Pratt
Publisher: WILEY
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Chapter 7, Problem 9E
Summary Introduction
To explain: Whether “Hemoglobin S homozygotes who are severely anemic often have elevated levels of BPG in their erythrocytes” is beneficial or not.
Concept introduction: Sickle cell disease is an autosomal recessive disorder that results in a type of anemia known as sickle cell anemia. The sickle cell disease is characterized by the HbS/HbS homozygous allele.
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Chapter 7 Solutions
Fundamentals of Biochemistry: Life at the Molecular Level
Ch. 7 - Prob. 1ECh. 7 - 2. Which set of binding data is likely to...Ch. 7 - Prob. 3ECh. 7 - Prob. 4ECh. 7 - 5. Drinking a few drops of a commercial...Ch. 7 - 6. Explain why long-distance runners prefer to...Ch. 7 - Prob. 7ECh. 7 - Prob. 8ECh. 7 - Prob. 9ECh. 7 - 10. In the variant hemoglobin C, glutamate at...
Ch. 7 - 11. Is myosin a fibrous protein or a globular...Ch. 7 - 12. In striated muscle, cells undergo mitosis...Ch. 7 - 13. A myosin head can undergo five ATP hydrolysis...Ch. 7 - 14. Rigor mortis, the stifle rung of muscles after...Ch. 7 - Prob. 15ECh. 7 - 16. Antibodies are well suited for recognizing...Ch. 7 - 17. Give the approximate molecular masses of an...Ch. 7 - 18. Many fish produce a tetrameric IgM. If each H...Ch. 7 - 19. Explain why the variation in VL and VH domains...Ch. 7 - 20. How many hypervariable loops are present in...Ch. 7 - Prob. 21CQCh. 7 - 22. If myoglobin had the same p50 value as...Ch. 7 - Prob. 23CQCh. 7 - Prob. 24CQCh. 7 - Prob. 25CQCh. 7 - Prob. 26CQCh. 7 - Prob. 27CQCh. 7 - Prob. 28CQCh. 7 - 29. Explain why a microfilament is polar, whereas...Ch. 7 - Prob. 30CQCh. 7 - Prob. 31CQCh. 7 - Prob. 32CQCh. 7 - Prob. 33CQCh. 7 - Prob. 34CQCh. 7 - MORE TO EXPLORE (a) Lock up information about...
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- 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 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_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_forward
- Below 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_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_forward
- The 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_forwardWhich peptide sequence is most likely to be found in the interior portion of a water-soluble globular protein? GGDGEMG DSKSTEG GAIVLWL IVAKSLIarrow_forward
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