Biochemistry
6th Edition
ISBN: 9781305577206
Author: Reginald H. Garrett, Charles M. Grisham
Publisher: Cengage Learning
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Chapter 16, Problem 10P
Interpretation Introduction
To determine:
The free energy difference represented by a Ca2+ gradient.
Introduction:
The mathematical expression for
Where
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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 Electrochemical Potential of a Sodium Ion Gradient Consider a phospholipid vesicle containing 10mM Na+ ions. The vesicle is bathed in a solution that contains 52mM Na+ ions, and the electrical potential difference across the vesicle membrane = outside- outside = -30mV. What is the electrochemical potential at 25C for Na+ ions?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. Quantitative Relationships Between Rale Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - II Triose phosphate isomerase catalyzes the conversion of glyceraldehyde-3-phosphate to dihydroxy-acetone phosphate. Glyceraldehyde3PdihydroxyacetonePThe Km of this enzyme tor its substrate glyceraldehyde-3-phosphate is 1.8 10-5 M. When [glyceraldehydes-3-phosphate] = 30 M, the rate of the reaction, v, was 82.5 mol mL-1 sec-1. a. What is Vmax for this enzyme? b. Assuming 3 nanomoles per mL of enzyme was used in this experiment ([Etotal]) = 3 nanomol/mL), what is kcat for this enzyme? c. What is the catalytic efficiency (kcat/Km) for triose phosphate isomerase? d. Does the value of kcat/Km reveal whether triose phosphate isomerase approaches catalytic perfection? e. What determines the ultimate speed limit of an enzyme-catalyzed reaction? That is, what is it that imposes the physical limit on kinetic perfection?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. Describe the Effects on cAMP and Glycogen Levels in Cells Exposed to Cholera Toxin Cholera toxin is an enzyme that covalently modifies the G-subunit of G proteins. (Cholera toxin catalyzes the transfer of ADP-ribose from NAD+ to an arginine residue in Gan ADP-ribosylation reaction.) Covalent modification of G� inactivates its GTPase activity. Predict the consequences of cholera to.vin on cellular cAMP and glycogen levels.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. Understanding Diffusion of Proteins in Membranes Protein lateral motion is much slower than that of lipids because proteins are larger than lipids. Also, some membrane proteins can diffuse freely through the membrane, whereas others art bound or anchored to other protein structures, in the membrane. The diffusion constant for the membrane protein fibronectin is approximately 0.7 X 10-12 cm/sec, whereas that for rhodopsin is about 3 X10-9 cm/sec. Calculate the distance traversed by each of these proteins in 10 msec. What could you surmise about the interactions of these proteins with other membrane components?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. 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.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. What properties of hyaluronate. chondroitin sulfate, and keratan sulfate make them ideal components of cartilage?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. 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.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_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 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_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. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - V Acetylcholinesterase catalyzes the hydrolysis of the neurotransmitter acetylcholine: Acetylcholine+H2Oacetate+cholineThe Km of acetylcholinesterase for its substrate acetylcholine is 9 10-5 M. In a reaction mixture containing 5 nanomoles/mL of acetylcholinesterase and 130 M acetylcholine, a velocity v0=40mol/mLsecwas observed for the acetylcholinesterase reaction. a. Calculate Vmax for this amount of enzyme. b. Calculate kcat for acetylcholinesterase. c. Calculate the catalytic efficiency (kcat/Km) for acetylcholinesterase. d. Does acetylcholinesterase approach catalytic perfection?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. Quantitative Relationships Between Rate Constants to Calculate Km, Kinetic Efficiency (kcat/Km) and Vmax - VI The enzyme catalase catalyzes the decomposition of hydrogen peroxide: 2H2O22H2O+O2The turnover number (kcat) for catalase is 40,000,000 sec-1. The Km of catalase for its substrate H2O2 is 0.11 M. a. In an experiment using 3 nanomole/L of catalase, what is Vmax? b. What is v when [H2O2] = 0.75 M? c. What is the catalytic efficiency of catalase? d. Does catalase approach catalytic perfection?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
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