Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 7, Problem 10P
Interpretation Introduction
Interpretation:
The chemical basis for the similarity in the caloric content values for carbohydrate and protein are to be stated.
Concept introduction:
Proteins are the
Carbohydrates are made up of elements, carbon, hydrogen and oxygen. They are one of the essential macronutrient in our diet. It is the major source of energy and is important for balanced diet.
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Biochemistry
Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Prob. 10P
Ch. 7 - Prob. 11PCh. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Prob. 14PCh. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Prob. 18PCh. 7 - Prob. 19PCh. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...Ch. 7 - Answers to all problems are at the end of this...
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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. 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.arrow_forwardAnswers 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?arrow_forwardAnswers 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.arrow_forward
- 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 Analysis of the blood of a catatonic football fan revealed large concentrations of a. psychologic octapeptide. Amino acid analysis of this oclapeplide gave the following results: 2 Ala lArg 1 Asp 1 Mel 2 Tyr I Val 1NH/ The following facts were observed: Partial acid hydrolysis of the octapeptide yielded a dipeptide of the structure Chymolrypsin treatment of the octapeplide yielded two tetrapeptides, each containing an alanine residue. Trypsin treatment of one of the tetrapeptides yielded two dipeptides. Cyanogen bromide treatment of another sample of the same tetrapeplide yielded a tripeplideand free Tyr. N-lerminal analysis of the other tetrapeptide gave Asn. What is the amino acid sequence of this oclapeplide?arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. A Rule of Thumb for Amino Acid Content in Proteins The simple average molecular weight of the 20 common amino adds is 138, but most biochemists use 110 when estimating the number of amino acids in a protein of known molecular weight. Why do you Suppose this is? (Hint: There are two contributing factors to the answer. One of them will be apparent from a brief consideration of the amino acid compositions of common proteins. See, for example, Figure 5.16 of this text.)arrow_forwardAnswers 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?arrow_forward
- 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.arrow_forwardAnswers to all problems are at the end οΓthis book. Detailed solutions are available in the Student Solutions Manual. Study Guide, and Problems Book. Enzymes and Y in the figure are both protein-digesting enzymes found in humans. Where would they most likely be at work? X is found in the mouth, Y in the small intestine. X in the small intestine. Y in the mouth. X in the stomach. Y in the small intestine. X in the small intestine. Y in the stomach.arrow_forwardAnswers to all problems are at the end of this book. Detailed solutions are available in the Student Solutions Manual, Study Guide, and Problems Book. Graphical Analysis of MWC Allosteric Enzyme Kinetics (Integrates with Chapter 1.1) Draw both Line weaver-Burk plots and Hanes-Woolf plots for an MWC allosteric enzyme system, showing separate curves for the kinetic response in (a) the absence of any effectors, (b) the presence of allosteric activator Λ, and (c) the presence of allosteric inhibitor I.arrow_forward
- 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 a decapeptide revealed the presence of the following products: The following facts were observed: Neither car boxy peptidase A nor B treatment of the- decapeptide had any effect. Trypsin treatment yielded two tetrapcptides and free Lys. Clostripain treatment yielded a tetrapcptide and a hexapeptidc. Cyanogen bromide treatment yielded an octapeptide and a dipeptide of sequence NP (using the one-letter codes). Chymotrypsin treatment yielded two tripeptides and a telrapeptide. The N-terminal chymotryptic peptide had a net charge of — 1 at neutral pi I and a net charge of —3 al pH 12. One cycle of Ed man degradation gave the PTH derivative What is the ammo acid sequence of this decapeptide?arrow_forwardAnswers 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.arrow_forwardAnswers 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 the pH of a Solution of a Weak Acid; Calculating the pH of the Solution after the Addition of Strong Base The ka for formic acid is 1.78 10-4 M. What is the pH of a 0.1 M solution of formic acid? 150 mL of 0.1 M NaOH is added to 200 mL of 0.1 M formic acid, and water is added to give a final volume of 1 L. What is the pH of the final solution?arrow_forward
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