EBK CAMPBELL BIOLOGY
11th Edition
ISBN: 8220103613828
Author: Reece
Publisher: PEARSON
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Chapter 8.4, Problem 4CC
Summary Introduction
To draw: A graph depicting the
Introduction: Lysosomes are the enzymes that are present in the cytoplasm and are used in breaking down of molecules such as carbohydrates. It also digests foreign agents during phagocytosis mechanism in many cellular organisms. It is also released during apoptotic reactions.
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Proteoglycan aggregates in tissues form hydrated, viscousgels. Can you think of any obvious mechanical reason whytheir capacity to form gels is important to cell function?[Hint: Liquid water is virtually incompressible.]
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concentration on the inside
AND
that it is_ to expect that the protein will at some point form a continuous path between th
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A outside
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O higher; unreasonable
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free energy
Chapter 8 Solutions
EBK CAMPBELL BIOLOGY
Ch. 8.1 - MAKE CONNECTIONS How does the second law of...Ch. 8.1 - Describe the forms of energy found in an apple as...Ch. 8.1 - WHAT IF? If you place a teaspoon of sugar in the...Ch. 8.2 - Cellular respiration uses glucose and oxygen,...Ch. 8.2 - VISUAL SKILLS How would the processes of...Ch. 8.2 - WHAT IF? Some nighttime partygoers wear glow-in-...Ch. 8.3 - How does ATP typically transfer energy from an...Ch. 8.3 - Prob. 2CCCh. 8.3 - MAKE CONNECTIONS Does Figure 8.11a show passive...Ch. 8.4 - Many spontaneous reactions occur very slowly. Why...
Ch. 8.4 - Prob. 2CCCh. 8.4 - WHAT IF? Malonate is an inhibitor of the enzyme...Ch. 8.4 - Prob. 4CCCh. 8.5 - How do an activator and an inhibitor have...Ch. 8.5 - Prob. 2CCCh. 8 - Explain how the highly ordered structure of a cell...Ch. 8 - Explain the meaning of each component in the...Ch. 8 - Describe the ATP cycle: How is ATP used and...Ch. 8 - How do both activation energy barriers and enzymes...Ch. 8 - Prob. 8.5CRCh. 8 - Choose the pair of terms that correctly completes...Ch. 8 - Prob. 2TYUCh. 8 - Which of the following metabolic processes can...Ch. 8 - Prob. 4TYUCh. 8 - Some bacteria art metabolically active in hot...Ch. 8 - If an enzyme is added to a solution where its...Ch. 8 - Prob. 7TYUCh. 8 - EVOLUTION CONNECTION Some people argue that...Ch. 8 - Prob. 9TYUCh. 8 - WRITE ABOUT A THEME: ENERGY AND MATTER Life...Ch. 8 - Prob. 11TYU
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- To approximate the concentration of enzymes in a bacterial cell, assume that the cell contains equal concentrations of 1,000 different enzymes in solution in the cytosol and that each protein has a molecular weight of 100,000. Assume also that the bacterial cell is a cylinder (diameter 1.0 μm, height 2.0 μm), that the cytosol (specific gravity 1.20) is 20% soluble protein by weight, and that the soluble protein consists entirely of enzymes. Calculate the average molar concentration of each enzyme in this hypothetical cell.arrow_forwardHow many copies of a protein need to be presentin a cell in order for it to be visible as a band on an SDSgel? Assume that you can load 100 μg of cell extract ontoa gel and that you can detect 10 ng in a single band by sil-ver staining the gel. The concentration of protein in cellsis about 200 mg/mL, and a typical mammalian cell has avolume of about 1000 μm3 and a typical bacterium a vol-ume of about 1 μm3. Given these parameters, calculatethe number of copies of a 120-kd protein that would needto be present in a mammalian cell and in a bacterium inorder to give a detectable band on a gel. You might try anorder-of-magnitude guess before you make the calcula-tions.arrow_forwardIn order to investigate the action of a bacterial membrane protein that is a light-driven proton pump, you purify the protein and assemble it together with phospholipids into liposomes that contain an indicator dye, which is blue at high pH, colorless at neutral pH, and red at low pH. You then expose the liposomes, in an aqueous solution, to sunlight. The interior of the liposomes turn blue. Further investigatin of the proton pump protein you find that treatment of either intact bacteria or the purified protein with the protease chymotrypsin result in cleavage of the protein at a single site near the amino terminus, which destroys its capacity to pump protons. When you treat the liposomes described above with chymotrypsin, the interior of the liposomes remains colorless. Create an illustration/ diagram of that illustrates the orientation of the pump protein in the plasma membrane of the intact bacterium and the direction in which it pumps protons.arrow_forward
- In order to investigate the action of a bacterial membrane protein that is a light-driven proton pump, you purify the protein and assemble it together with phospholipids into liposomes that contain an indicator dye, which is blue at high pH, colorless at neutral pH, and red at low pH. You then expose the liposomes, in an aqueous solution, to sunlight. The interior of the liposomes turn blue. Further investigatin of the proton pump protein you find that treatment of either intact bacteria or the purified protein with the protease chymotrypsin result in cleavage of the protein at a single site near the amino terminus, which destroys its capacity to pump protons. When you treat the liposomes described above with chymotrypsin, the interior of the liposomes remains colorless. From these results create a diagram of that illustrates the orientation of the pump protein in the plasma membrane of the intact bacterium and the direction in which it pumps protons. Explain your reasoning.arrow_forwardWhat is the expected outcome of the ion exchange chromatography using lysozyme as outlined above? Will the protein be separated successfully or not using the materials stated in the above? Provide a brief explanation to your reasoning please answer correctly, not written assigmentarrow_forwardUsing the the enzyme acid hydrolase in the lysosome: What is the final destination in which the protein will function? Which features will the protein receive during its manufacture? What is the primary structure (general)? Where is the primary structure made? Where are the secondary and tertiary structures made? Will the protein travel through any organelles during its manufacture? Which ones? What would be the overall result if some part of the manufacture process went wrong, such that the protein ended up as nonfunctional?arrow_forward
- The antibiotic Gramicidin A can transport Na+ inons into a certain cell at the rate of 5.0 x 10 ^7 Na+ ion channel-1 s-1. Calculate the time in seconds it takes to transport enough Na+ ions to increases its concentration by 8.0 x10 -3 M in a cell whose intracellular volume is 2.0 x 10-10 mLarrow_forwardMatch the letter in the diagram with the accumulation or localization of active (or about to be active) protein in a given cellular context, which is wild-type unless specified. CYTOSOL EXTRACELLULAR SPACE A 1. M6P receplor bound to ligand 2. a protein with an (N-SIG] only in a class E yeast mutant 3. plasma membrane v-SNARE 4, clathrinarrow_forward(c) The tube and cylinder diagram to the right illus- trates schematically the potassium channel protein from a bacterium. This channel protein consists of four identical polypeptide chains each comprised of 119 residues. The cyan ribbon illustrates only two of the polypeptide chains. The relative positions of 4 α-helices, one from each poly- peptide chain, are shown as cylinders. The red sphere in the central part of the diagram shows the position of a potas- sium ion identified by X-ray structure analysis. A cesium ion (green sphere) was also found to be stabilized in the same position when cesium chloride was introduced into the crys- tals. The cylinders each represent an α-helix running from Tyr62 to Thr74. Considering the position of the potassium ion, in- dicate on one of the cylinders at which end of the cylinder residue Tyr62 is found and at which end residue Thr74 is found. Explain the basis of your answer? Ala23 Thr119 (d) The N- and C-terminal residues of one of the…arrow_forward
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