Biochemistry
Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 2, Problem 13P

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.

How to Prepare a Buffer Solution: a HEPES Buffer Given a solution of 0.1 M HEPES in its fully protonated form and ready access to 0.l M HCl, 0.1 M NaOH, and distilled water, describe the preparation of 1 L of 0.025 M HEPES buffer solution, pH 7.8.

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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. Preparing a Phosphate Buffer Solution of pH 7.5 from Solutions of Na3PO4 and H3PO4 Given 0.1 M solutions of Na3PO4, and H3PO4 describe the preparation of 1 L of a phosphate buffer at a pH of 7.5. What are the molar concentrations of the ions in the final buffer solution, including Na+ and H+?
    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. Prepare a Buffer by Combining a Solution of Weak Acid with a Solution of the Salt of the Weak Acid Given 0.1 M solutions of acetic acid and sodium acetate, describe the preparation of 1 L of 0.1 M acetate buffer at a pH of 5.4.
  • 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. Interpreting Kinetics Experiments from Graphical Patterns The following graphical patterns obtained from kinetic experiments have several possible interpretations depending on the nature of the experiment and the variables being plotted. Give at least two possibilities for each.
    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.
    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. Phosphorylation of Proteins Introduces New Properties Phosphoproteins are formed when a phosphate group is esterified to an —OH group df a Ser, Thr, or Tyr side chain. At typical cellular pH values, this phosphate group bears two negative charges (— OPO32:_). Compare this side-chain modification to the 2U side chains of the Common amino acids found in proteins and comment on the novel properties that it introduces into side-chain possibilities.
    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. How to Prepare a Buffer Solution: An Anserine Buffer Draw the titration curve for anserine (Figure 2.16). The isoelectric point of anserine is the pH where the net charge on the molecule is zero: what is the isoelectric point for anserine? Given a 0.1 M solution of anserine at its isoelectric point and ready access to 0.1 M HCl, 0.1 M NaOH, and distilled water, describe the preparation of 1 L of 0.04 M anserine buffer solution. pH 7.2.
    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 [H] and pKd from the pH of a Solution of Weak Acid The pH of a 0.02 M solution of an acid was measured at 4.6. What is the [H+] in this solution? Calculate the acid dissociation constant Ka and pKa for this acid.
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