CAMPBELL BIOLOGY-MASTERING BIO.ACCESS
12th Edition
ISBN: 9780136486787
Author: Urry
Publisher: SAVVAS L
expand_more
expand_more
format_list_bulleted
Concept explainers
Videos
Textbook Question
Chapter 6.7, Problem 3CC
MAKE CONNECTIONS Ø 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 5.14, what would you predict about the amino acid sequence of the tight junction protein?
Expert Solution & Answer
Want to see the full answer?
Check out a sample textbook solution
Students have asked these similar questions
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…
1. 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
Cytosol
+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.
Chapter 6 Solutions
CAMPBELL BIOLOGY-MASTERING BIO.ACCESS
Ch. 6.1 - Prob. 1CCCh. 6.1 - Prob. 2CCCh. 6.2 - Briefly describe the structure and function of the...Ch. 6.2 - DRAW IT Draw a simplified elongated cell that...Ch. 6.3 - What role do ribosomes play in carrying out...Ch. 6.3 - Describe the molecular composition of nucleoli and...Ch. 6.3 - Prob. 3CCCh. 6.4 - Describe the structural and functional...Ch. 6.4 - Describe how transport vesicles integrate the...Ch. 6.4 - WHAT IF? Imagine a protein that functions in the...
Ch. 6.5 - Describe two characteristics shared by...Ch. 6.5 - Prob. 2CCCh. 6.5 - Prob. 3CCCh. 6.6 - Prob. 1CCCh. 6.6 - WHAT IF? Males afflicted with Kartagener's...Ch. 6.7 - In what way are the cells of plants and animals...Ch. 6.7 - Prob. 2CCCh. 6.7 - MAKE CONNECTIONS The polypeptide chain that makes...Ch. 6.8 - Prob. 1CCCh. 6 - Prob. 6.1CRCh. 6 - Explain how the compartmental organization of a...Ch. 6 - Describe the relationship between the nucleus and...Ch. 6 - Describe the key role played by transport vesicles...Ch. 6 - What does the endosymbiont theory propose us the...Ch. 6 - Describe the role of motor proteins inside the...Ch. 6 - Prob. 6.7CRCh. 6 - When a cell ingests a bacterium, what role does...Ch. 6 - Prob. 1TYUCh. 6 - Prob. 2TYUCh. 6 - Which of the following is present in a prokaryotic...Ch. 6 - Prob. 4TYUCh. 6 - Which cell would be best for studying lysosomes?...Ch. 6 - Prob. 6TYUCh. 6 - EVOLUTION CONNECTION (a) What cell structures best...Ch. 6 - SCIENTIFIC INQUIRY Imagine protein X, destined to...Ch. 6 - WRITE ABOUT A THEME: ORGANIZATION Considering some...Ch. 6 - SYNTHESIZE YOUR KNOWLEDGE The cells in this SEM...
Additional Science Textbook Solutions
Find more solutions based on key concepts
Why are mutants used as test organisms in the Ames test?
Laboratory Experiments in Microbiology (12th Edition) (What's New in Microbiology)
Describe the evolution of mammals, tracing their synapsid lineage from early amniote ancestors to true mammals....
Loose Leaf For Integrated Principles Of Zoology
Sea turtles have disappeared from many regions, and one way of trying to save them is to reintroduce them to ar...
Marine Biology (Botany, Zoology, Ecology and Evolution)
WHAT IF? As a cell begins the process of dividing, its chromosomes become shorter, thicker, and individually vi...
Campbell Biology in Focus (2nd Edition)
Review the Chapter Concepts list on page 422. These all center on quantitative inheritance and the study and an...
Essentials of Genetics (9th Edition) - Standalone book
Knowledge Booster
Learn more about
Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- Biological membranes are critical components of cells that allow compartmentalisation of cellular contents. The diagram shows a biological membrane comprised of a lipid bilayer with a single polypeptide integrated into the membrane and spanning the membrane seven times. What types of amino acids are likely present in the parts of the polypeptide chain labelled 1-7 and in the parts of labelled A-G? What is the name of the effect that forces the polypeptide to arrange itself like this within the lipid bilayer? Give an example of a type of molecule that can move freely across the lipid bilayer and explain why it can do so based on its chemical properties.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_forwardDrawn below is a schematic of a transmembrane protein. Extracellular Cell membrane Cytosolic side (a) When this transmembrane protein is embedded in the lipid bilayer, what is the highest order of structure (choose from primary, secondary, tertiary and quaternary) of this protein? Explain why you selected this option.arrow_forward
- B) We also know from studies of protein structure that one turn of an a-helix includes 3.6 amino acid residues and extends the long axis of the helix by - 0.56 nm. Approximately how many amino acids must a helical transmembrane segment of an integral membrane protein have if the segment is to span the lipid bilayer defined by two stearate molecules laid end to end, plus the polar head groups to which the stearate molecules are attached (assume a polar head group has a diameter of 0.5 nm)?arrow_forwardI'm honestly confused on where to start with this question. I think it has something to do with the residues per turn but can you please explain and show detailed work on the the problem. Researchers have discovered a new membrane protein that has three transmembrane domain αhelixes that span the lipid bilayer. a. If the lipid bilayer is 30 Å thick, what is the smallest number of amino acid residues that can be in each α-helixes for them to be long enough to span the bilayer? b. If one of the three α-helixes is titled at a 32° angle relative to an axis perpendicular to the surface of the lipid bilayer, what is the smaller number of amino acid helixes required for that helix to still span the lipid bilayer? c. How many hydrogen bonding interactions would there be in the smallest possible tilted transmembrane α-helix? d. If the tilted α-helix was a 310 helix instead how many amino acid residues would be required to span the lipid bilayer? How many amino acid residues would be required if…arrow_forwardChoose the statements that describe how the helix orients in the tertiary structure of an integral membrane protein. The threonine residues act as membrane interface anchors, interacting with the lipid bilayer and the aqueous environment. The amphipathic helix interacts with the lipid bilayer along its hydrophobic surface, exposing its hydrophilic surface to the aqueous environment. A group of helices cluster with their polar surfaces in contact with one another and their hydrophobic surfaces facing the lipid bilayer. The peptide entirely embeds in the lipid bilayer. Incorrectarrow_forward
- Using 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_forwardMonomeric, single-pass transmembrane proteins span a membrane with a single a helix that has characteristic chemical properties in the region of the bilayer. Which of the three 20-amino-acid sequences listed below is the most likely candidate for such a transmembrane segment? O TLIYFGVMAGVIGTILLIS O ITPIYFGPMAGVIGTPLLIS ITEIYFGRMAGVIGTDLLISarrow_forwardWhere is the KV1.1 (a membrane protein) polypeptide synthesized in the cell? (word bank: cytoplasm, nucleus, rough ER, smooth ER, mitochondria) The amino acids that line the outside of the KV1.1 protein (i.e., those in contact with the phospholipid bilayer's fatty acids tails) are more likely to be _______(word bank: hydrophobic, hydrophilic) The KV1.1 protein utilizes __ transport to move the K+ ions across the membrane. (word bank: active, passive) This disease can be caused by missense mutations. In general, how specifically would a missense mutation affect the KV1.1 protein?arrow_forward
- Proteins that span the biological membrane bilayers often contain α-helices and b-barrels. (a) Given that the insides of membranes are highly hydrophobic, predict what type of amino acyl residues would be found in a single alpha-helix that is spanning a membrane – draw a diagram to illustrate the arrangement of the R-groups within the membrane bilayer. (b) Using a drawing, illustrate the R-group arrangement in the membrane-spanning region of a channel protein for water transport if the channel was made of: six alpha-helices six beta-strandsarrow_forwardRoughly sketch the hydropathy plot for the given hypothetical membrane protein. Follow the color assignment of the helical domains and properly label your plot and axes (NB: Only a rough sketch is being asked. No need be exact with the hydropathy indices and residue numbers). CO-arrow_forwardThe 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_forward
arrow_back_ios
SEE MORE QUESTIONS
arrow_forward_ios
Recommended textbooks for you
Biology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStax
Biology: The Unity and Diversity of Life (MindTap...BiologyISBN:9781305073951Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa StarrPublisher:Cengage Learning
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Biology: The Unity and Diversity of Life (MindTap...
Biology
ISBN:9781305073951
Author:Cecie Starr, Ralph Taggart, Christine Evers, Lisa Starr
Publisher:Cengage Learning
Types of Human Body Tissue; Author: MooMooMath and Science;https://www.youtube.com/watch?v=O0ZvbPak4ck;License: Standard YouTube License, CC-BY