Campbell Biology in Focus (2nd Edition)
2nd Edition
ISBN: 9780321962751
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece
Publisher: PEARSON
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Chapter 4.7, Problem 3CC
MAKE CONNECTIONS The polypeptide chain that makes up a tight junction weaves back and forth through the membrane four times, with two extracellular loops, and one loop plus short C-terminal and N-terminal tails in the cytoplasm. Looking at Figure 3.18, whatWhat would you predict about the amino acids making up the tight junction protein?
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25. Your friend works in a cell biology research lab. She is working
she calls p125, because its molecular mass is 125 kiloDaltons. She knows that
p125 is a transmembrane protein with three membrane-spanning domains. It has
been previously reported that p125 interacts with three other proteins called p175,
p80, and p50 (again,
polyacrylamide gel). These four proteins
in the cell. To determine how these proteins interact with the membrane, you
perform a set of experiments in which you first lyse the cells and save some of
your lysate, which you run in the input lane (labeled "I" in Figure Q25 below).
The lysate is then subjected to a low-speed centrifugation so that you separate out
the membrane fraction (which ends up in the pellet, "P") from the cytoplasm
(which is in the supernatant, "S"). You then wash the pellet from the first
extraction with a high-salt wash that does not disrupt the lipid bilayer, and save a
little bit to run on the gel. After the high-salt wash, you centrifuge…
Drawn below is a schematic of a transmembrane protein.
Extracellular
Cell
membrane
Cytosolic side
(a) From the list below, select the amino acid(s) that might by more common in the extracellular domain of
this membrane protein and whose side- chain can form hydrogen bonds with the surrounding water
molecules. Explain why you selected this option(s).
Lysine
Serine
Phenylalanine
Methionine
(b) From the list below, select the amino acid(s) that would likely be found in the transmembrane/
membrane spanning domain of this protein and whose side- chain interacts with the lipid bilayer.
Lysine
Serine
Phenylalanine
Methionine
Explain how the amphipathic (containing both hydrophobic and hydrophilic sides) protein (shown; left)would be anchored in the phospholipid bilayer (shown; right); which portion do you predict would besticking out towards the water? Which portion would be hiding inside the membrane?
Chapter 4 Solutions
Campbell Biology in Focus (2nd Edition)
Ch. 4.1 - Prob. 1CCCh. 4.1 - Prob. 2CCCh. 4.2 - Briefly describe the structure and function of the...Ch. 4.2 - Prob. 2CCCh. 4.3 - What role do ribosomes play in carrying out...Ch. 4.3 - Describe the molecular composition of nucleoli,...Ch. 4.3 - WHAT IF? As a cell begins the process of dividing,...Ch. 4.4 - Describe the structural and functional...Ch. 4.4 - Describe how transport vesicles integrate the...Ch. 4.4 - WHAT IF? Imagine a protein that functions in the...
Ch. 4.5 - Describe two characteristics shared by...Ch. 4.5 - Prob. 2CCCh. 4.5 - Prob. 3CCCh. 4.6 - Prob. 1CCCh. 4.6 - WHAT IF? Males afflicted with Kartageners syndrome...Ch. 4.7 - In what way are the cells of plants and animals...Ch. 4.7 - Prob. 2CCCh. 4.7 - MAKE CONNECTIONS The polypeptide chain that makes...Ch. 4 - Which structure is not part of the endomembrane...Ch. 4 - Which structure is common to plant and animal...Ch. 4 - Which of the following is present in a prokaryotic...Ch. 4 - Prob. 4TYUCh. 4 - Cyanide binds to at least one molecule involved in...Ch. 4 - What is the most likely pathway taken by a newly...Ch. 4 - Which cell would be best for studying lysosomes?...Ch. 4 - DRAW IT From memory, draw two eukaryotic cells....Ch. 4 - SCIENTIFIC INQUIRY In studying micrographs of an...Ch. 4 - FOCUS ON EVOLUTION Compare different aspects of...Ch. 4 - FOCUS ON ORGANIZATION Considering some of the...Ch. 4 - Prob. 12TYU
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- * hat do you think holds together the various secondary structural elements in a Particular three-dimensional pattern? (Hint: Look back at Figure 4 - what is sticking out from the sides of the a-helices and B-strands?) glutamic acid B CH, CH valine CH H-N CH H. valine alanine CH2 CH2 lysine Figure 4-4 Essential Cell Biology 3/e (O Garland Science 2010) Figure 6. Three examples of bonding interactions that stabilize the tertiary structures of proteins (indicated by arrows A, B,and C). Copyright 2013 from Essential Cell Biology, 4th Edition by Alberts et al. Reproduced by permission Garland Science/ Taylor & Francis LLC. CH2 CH, SH SH CH2 CH2 OXIDATION CH2 SH REDUCTION SH CH2 CH2 Figure 4-26 Essential Cell Bialogy 3e o Garland Science 2010) Figure 7. Disulfide bonds within proteins can form (left-pointing arrow) or be broken (right- pointing arrow), depending on their chemical surroundings (oxidative or reducing). Copyright 2013 from Essential Cell Biology,4th Edition by Alberts et al.…arrow_forward+H₂N-CH-COO™ 1 CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. amino acid D O amino acid B amino acid C O amino acid A +H₂N-CH-COO™ 1 amino acid E C=O B. Of the four amino acids shown, this amino acid would most likely be located in the transmembrane domain of an integral membrane protein. +H₂N-CH-COO™ 1 CH₂ 1 OH C. +H₂N-CH-COO™ I CH H₂C CH₂ D.arrow_forward1. Integral and peripheral membrane proteins employ multiple strategies to keep them associated to a biological membrane. View these three proteins below, and for each protein shown, answer the following questions: A) What type of membrane protein is this? Integral, peripheral, monotopic, polytopic? How do you know? Justify your label by features of the protein shown in the image. B) Describe the overall tertiary structure of each protein. Be certain to mention hydrophilicity/hydrophobicity of the surfaces of this protein. C) Provide a detailed description of how each protein is held associated to the biological membrane. Protein 2 Protein 3 Protein 1 "H,N. Exterior Cytosolarrow_forward
- Look carefully at the transmembrane proteins shown in Figure 11–29. What can you say about their mobility in the membrane?arrow_forwardSuppose that you joined a group of scientists working with a multipass ER-resident membrane protein. By only analyzing the amino acid sequence, how can you determine the number of transmembrane portions that the protein has? How can you determine whether the N-terminus is at the cytosolic side or at the ER lumen side?arrow_forwardn addition to transmembrane a-helices another type of polypeptide structure of Integral membrane proteins that extends through the lipid bilayer is: segments with mainly charged amino acids B barrel segments with mainly polar amino acids single B-strand irregular secondary structure d)arrow_forward
- The lipid portion of a typical bilayer is about 30 Å thick. (a) Calculate the minimum number of residues in an a-helix required to span this distance. (b) Calculate the minimum number of residues in a B-strand required to span this distance. (c) Explain why a-helices are most commonly observed in transmembrane protein sequences when the distance from one side of a membrane to the other can be spanned by significantly fewer amino acids in a B-strand conformation. (d) The epidermal growth factor receptor has a single transmembrane helix. Find it in this partial sequence: .RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH..arrow_forwardWhile investigating structure-function studies in a membrane transport protein, a researcher discovered a single nucleotide mutation that led to the loss of a key alpha-helical segment of the protein in the hydrophilic domain. The mutation that led to this finding is most likely which of the following? Hint: helix breaker O AUC to GUC GAG to CCU GUU to GCU GUG to UUG O CUC to CCCarrow_forwardThe integral membrane protein XYZR has a single alpha helix spanning the membrane. Where was this protein made and what can you say about amino acids that occur/do not occur in the alpha helix versus the domains sticking out on both sides of the membrane?arrow_forward
- Order following for rate of diffusion through a synthetic lipid bilayer. Explain your order. Cl-, N2, alanine, tRNA, ribose, H2Oarrow_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_forwardName the three major assumptions made by the "Cell theory". (i) The lipid membrane is composed of lipid molecules. Explain the principle of membrane formation highlighting the role of the physical properties of the lipids. (ii) Comparing dimensions and length scales is often a first step in an analysis. Give an approximate value for the thickness of a lipid bilayer and the linear length of a helical turn of a DNA double helix. A technician wants to amplify DNA from a patient sample. However, the lab is not equipped with a thermocycler. (i) (ii) Name two methods for DNA amplification that can be operated at constant temperature and give their acronyms. Explain these two methods in detail using a schematic and name all necessary components that are required to perform the amplification. Describe the main function of the middle ear. Highlight the role of the ossicles and the tympanic membrane.arrow_forward
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