Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 9, Problem 6P
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.
- Understanding the Phase Transitions of Membrane Phospholipids
Discuss the effects on the lipid phase transition of pure dimyristoyl phosphatidylcholine vesicles of added (a) divalent cations, (b) cholesterol, (c) distearoyl phosphatidylscrine. (d) dioleoyl phosphatidylcholine, and (e) integral meinbrane proteins.
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Chapter 9 Solutions
Biochemistry
Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Prob. 4PCh. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...Ch. 9 - Answers to all problems are at the end of this...
Ch. 9 - Prob. 11PCh. 9 - Prob. 12PCh. 9 - Answers to all problems are at the end of this...Ch. 9 - Prob. 14PCh. 9 - Prob. 15PCh. 9 - Prob. 16PCh. 9 - Answers to all problems are at the end of this...Ch. 9 - Prob. 18PCh. 9 - Prob. 19PCh. 9 - Prob. 20PCh. 9 - Prob. 21PCh. 9 - Prob. 22PCh. 9 - Prob. 23PCh. 9 - Prob. 24PCh. 9 - Answers to all problems are at the end of this...Ch. 9 - Prob. 26PCh. 9 - Prob. 27PCh. 9 - Prob. 28PCh. 9 - Prob. 29PCh. 9 - Prob. 30PCh. 9 - Prob. 31P
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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. 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?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 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. 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_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 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_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. 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_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. 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_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. Comparing Membrane Barrel Structures Compare the porin proteins, which have transmembrane pores constructed from -barrels, with the Wza protein, which has a transmembrane pore constructed from a ring of -helices. How many amino acids are required to form the -barrel of a porin? How many would be required to form the same-sized pore from -helices?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. Determining the Length of a Keratin Molecule The central rod domain of a keratin protein is approximately 312 residues in length. What is the length (in A) of the keratin rod domain? If this same peptide segment were a true -helix how long would it be? If the same segment were a -sheet, what would its length be?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. Calculating the Molecular Weight and Subunit Organization of a Protein From Its Metal Content The element molybdenum {atomic weight 95.95) constitutes 0.0K if the weight of nitrate reductase. If the molecular weight of nitrate reductase is 240,000, what is its likely quaternary structure?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. (Research Problem) The Nature and Roles of Linear Motifs in Proteins In addition to domains and modules, there are other significant sequence patterns in proteins—known as linear motifs—that are associated with a particular function. Consult the biochemical literature to answer the following questions: 1. What are linear motifs? 2. How are they different from domains?. 3. What are their functions? 4. How can they be characterized? 5. There are several papers that are good starting points for this problem. Neduva, V., and Russell, R., 2005. Linear motifs: evolutionary interaction switches. FEBS Letters 579:3342-3345. Gibson, T., 2009. Cell regulation: determined to signal discrete cooperation. Trends in Biochemical Sciences 34:471-482. Diella, K. Haslam, N., Chica., C. et aL, 2009. Understanding eukaryotic linear motifs and their role in cell signaling and regulation. Frontiers of Bioscience 13:6580-6603.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
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