Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 7, Problem 3P

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.

Separating Glycated Hb From Normal Hb (Integrates with Chapters 5 and 6.) Human hemoglobin can react with sugars in the blood (usually glucose) to form covalent adducts. The α-amino groups of N-terminal valine in the Hb β-subunits react with the C-1 (aldehyde) carbons of monosaceharides to form aldimine add wets, which rearrange to form very stable ketoamine products. Quantitation of this “glycated hemoglobin" is important clinically, especially for diabetic individuals. Suggest at least three methods by which glycated lib (also referred to as HbA1c) could be separated from normal Hb and quantitated.

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  • 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. Solving the Sequence of an Oligopeptide From Sequence Analysis Data Amino acid analysis of ail oligopeptide seven residues long gave The following fads were observed: a. Trypsin treatment had no apparent effect. b. The phenylthiohydantoin released by Lid mini degradation was c. Brief chymotrypsin treatment yielded several products, including a dipeptide and a tetrapeptide. The amino acid composition of the tetrapeptide was Leu, Lyi. and Met. d. Cyanogen bromide treatment yielded a dipeptide, a tetrapeptide, and free Lys. What is the amino acid sequence of this heptapeptide?
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    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. The Biosynthetic Capacity of Cells The nutritional requirements of Escherichia coli cells are far simpler than those of humans, yet the macromolecules found in bacteria are about as complex as those of animals. Because bacteria can make all their essential biomolecules while subsisting on a simpler diet, do you think bacteria may have more biosynthetic capacity and hence more metabolic complexity than animals? Organize your thoughts on this question, pro and con, into a rational argument. (Section 1.5)
  • 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. Evaluation of -Helices in Proteins The hem agglutinin protein in influenza virus contains a remarkably long -helix, with 53 residues. How long is this -helix (in nm)? How many turns does this helix have? The typical residue in an -helix is involved in two H bonds. How many H bonds are present in this helix?
    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. Use examples from the ActiveModel for Human GaleLtin-1 to describe the hydrophobic effect.
    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. Assessing the Effect of Temperature on Equilibrium You are studying the various components of the venom of a poisonous lizard. One of the venom components is a protein that appears to be temperature sensitive. When heated, it denatures and is no longer toxic. The process can be described by the following simple equation: There is only enough protein from this venom to carry out two equilibrium measurements. At 298 K, you find that 98% of the protein is in its to.\ic form. However, when you raise the temperature to 320 �.. you find that only 10% of the protein is in its toxic form. Calculate the equilibrium constants for the T to N conversion at these two temperatures. Use the data to determine the H,S, and G for this process.
  • 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. Draw the Titration Curve for a Weak Acid and Determine its pKa from the Titration Curve When a 0.1 M solution of a weak acid was titrated with base, the following results were obtained: Plot the results of this titration and determine the pK a of the weak acid from your graph.
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    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. Plot the Titration Curve for Bicine and Calculate How to Prepare a pH 7.5 Bicine Buffer Solution Bicine (N, N—bis (2-hydroxyethyl) glycine) is another commonly used buffer in biochemistry labs. The structure of Bicine in its fully protonated form is shown here: Draw the titration curve for Bicine. assuming the pA'a for its free COOH group is 2.3 and the pAa for its tertiary amino group is 8.3. Draw the structure of the fully deprotonated form (completely dissociated form) of bicine. You have available a U.l Msolution of Bicine at its isoelectric point (pH|)T 0.1 M solutions of HCI and NaOH. and ample distilled water. Describe the preparation of 1 L of 0.U4 M Bicine buffer. pH 7.5. What is the concentration of the fully protonated form of Bicine in your final buffer solution?
  • 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. Determining the Branch Points and Reducing Ends of Amylopectin A 0.2-g sample of amylopectin was analyzed to determine the fraction of the total glucose residues, that are branch points in the structure. The sample was exhaustively methylated and then digested, yielding 50-mol of 2,3-dimethylgluetose and 0.4 mol of 1,2,3,6- letramethylglucose. What fraction of the total residues are branch points? I low many reducing ends does this sample of amylopectin have?
    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. Table 5.4 presents some of the many known mutations in the genes encoding the a- and -globin subunits of hemoglobin. a. Some of these mutations affect subunit interactions between the Subunits. In an examination of the tertiary structure of globin chains, where would you expect to find amino acid changes in mutant globins that affect formation of the hemoglobin 22quaternary structure? b. Other mutations, such as the S form of the-globin chain, increase the tendency of hemoglobin tetramers to polymerize into very large structures. Where might you expect the amino acid substitutions to be in these mutants?
    Answers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Superbug infections are becoming more common around the world. Many of these infections arise from the action of -lactamases, of which there are several types with different mechanisms of action. Consult the end-of-chapter reference by von Nussbaum and Schiffer and write detailed mechanisms for the serine -lactamases and metallo- -lactamases.
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