Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 5, Problem 12P
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.
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Chapter 5 Solutions
Biochemistry
Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - Answers to all problems are at the end of this...Ch. 5 - 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. (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_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. 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?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. 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. 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. General Controls Over Enzyme Activity List six general ways in which enzyme activity is controlled.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. 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. Use examples from the ActiveModel for Human GaleLtin-1 to describe the hydrophobic effect.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 Composition of Anomeric Sugar Mixtures -D-Glucose has a specific notation, []220, of + 112.20. whereas -D-glucose has a specific notation of +18.70. What is the composition of a mixture of - and -D-glucose, which has a specific notation of 83 .U0?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 an oligopeptide containing nine residues revealed the presence of the following amino adds: Arg Cys Gly Leu Met Pro Tyr Val The following was found: Carboxypeptidase A treatment yielded no free amino add. Edman analysis of the intact oligopeptide released c. Neither trypsin nor ehymotrypsin treatment of the nonapeptide released smaller fragments. However, combined trypsin and chymotrypsin treatment liberated free Arg. CNBr treatment of the eight-residue fragment left after combined trypsin and chymotrypsin action yielded a six-residue fragment containing Cys* Gly. Pro, Tyr, and Val and a dipeptide. Treatment of the six-residue fragment with -mercaptoethanol yielded two tripeptidcs. Brief Edman analysis of the tripeplide mixture yielded only Ρ�Ή-Cys. (The sequence of each tripeptide, as read from the N-terminal end, is alphabetical if the one-lelter designation for amino acids is used.) What is the amino acid sequence of this nonapeptide?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. The dissociation constant for a particular protein dimer is 1 micromolar. Calculate the free energy difference for the monomer-to-dimer transition.arrow_forward
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