When fluorescein-dyed human proteins were first mixed with rhodamine-dyed mouse proteins (in mouse/human hybrid cell fusions carried out in the 1970s), these proteins appeared to exhibit: restricted movement, based on confinement by diffusion barriers restricted movement, based on tethering to extracellular molecules unrestricted movement, similar to membrane phospholipids restricted movement, based on anchoring to intracellular proteins restricted movement, based on attachment to other cells

When fluorescein-dyed human proteins were first mixed with rhodamine-dyed mouse proteins (in mouse/human hybrid cell fusions carried out in the 1970s), these proteins appeared to exhibit: restricted movement, based on confinement by diffusion barriers restricted movement, based on tethering to extracellular molecules unrestricted movement, similar to membrane phospholipids restricted movement, based on anchoring to intracellular proteins restricted movement, based on attachment to other cells

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter9: Cell Communication

Section: Chapter Questions

Problem 3ITD

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When rhodamine-dyed mouse proteins were first mixed with fluorescein-dyed human proteins (in mouse/human hybrid cell fusions), these proteins appeared to exhibit: restricted movement, based on confinement by diffusion barriers restricted movement, based on tethering to extracellular molecules unrestricted movement, similar to membrane phospholipids restricted movement, based on anchoring to intracellular proteins restricted movement, based on attachment to other cells
A peripheral protein, which is not integral to the cell membrane, is also called: a multi-pass transmembrane protein (like band 3.0 protein) a single-pass transmembrane protein (like glycophorin A) a monolayer-associated protein (like the COX-1 protein) a protein-attached protein (like cytochrome c) a lipid-linked protein (like the Ras protein)
Which of these answers explains why synaptic vesicles only releasee their neurotransmitter cargo in response to a signal? A) the necessary Rab proteins are not synthesized until an action potential arrives B) vesicle formation at the trans-Golgi network cannot occur in the absence of plasma membrane depolarization C) an additional protein, synaptotagmin, makes vesicle fusion dependent on the calcium concentration D)a plasma membrane transporter is needed to actively pump neurotransmitter into the synaptic cleft. These are inactive until membrane depolarization
Focal adhesion complex attachment to extracellular matrix molecules is mediated by: heterodimers of alpha-integrin and beta integrin homodimers of classical cafherins The force of gravity actin filaments
Microtubules are important for transporting cargo in nerve cell axons, as diagrammed in Figure Q17- 33. Notice that the two types of cargo are traveling in opposite directions. Which of the following statements is likely to be false? cell body microtubule axon Figure Q17-33 inward transport axon terminal The black cargo and the gray cargo require ATP hydrolysis for their motion. The gray cargo is attached to dynein. outward transport The black cargo and the gray cargo are moving along microtubules of opposite polarity. The black cargo moving toward the axon terminal contains a domain that specifically interacts with the tail domain of a particular kind of motor.
For each of the following scenarios described where a molecule or ion is moving from one side of a membrane to the other, select the method by which the molecule or ion is moving. Each answer can be used more than once, or not at all. - Simple Diffusion - Facilitated diffusion by a channel protein - Facilitated diffusion by a carrier/transport protein - Active transport by a pump - Could be facilitated diffusion by a channel or a carrier; not enough information is given A- While water can freely diffuse across the membrane, it does not do so fast enough for living organisms to function properly. Therefore, membrane proteins known as aquaporins can increase the rate at which water moves across the membrane. The movement of water across the membrane via aquaporins (which do not change shape) is an example of which type of transport? B-Many snake venoms induce paralysis by acting on acetylcholine receptors. Nicotinic acetylcholine receptors are transmembrane proteins that allow Na+, K+…
8) Indicate which of the five major types of membrane protein (adhesion, enzymatic, recognition, receptor, and transport) is most likely to be involved in each of the situations described below: a) An oncologist wants to study the cells from a certain tumour that has been surgically removed from a patient. However, she must first treat the tumour with a solution affects a membrane protein on the tumour cells. Because of the effect of the solution on the membrane protein, the tumour tissue falls apart into individual cells. Type of membrane protein: b) Farmer Jebediah wakes up in the morning and makes himself an extra-strong coffee. The caffeine in the coffee attaches to a protein in the plasma membrane of his neurons, inducing a signal transduction cascade and causing Farmer Jebediah to be more alert Type of membrane protein:
A transmembrane protein has the following properties: it has two binding sites, one for solute A and one for solute b. The protein can undergo a conformational change to switch between two states: either both binding sites are exposed exclusively on one side of the membrane or both binding sites are exposed exclusively on the other side of the membrane. The protein can switch between the two conformational states only if both binding sites are occupied or if both binding sites are empty, but cannot switch if only one binding site is occupied. What kind of protein do these properties define?
A transmembrane protein has the following properties: it has two binding sites, one for solute A and one for solute b. The protein can undergo a conformational change to switch between two states: either both binding sites are exposed exclusively on one side of the membrane or both binding sites are exposed exclusively on the other side of the membrane. The protein can switch between the two conformational states only if both binding sites are occupied or if both binding sites are empty, but cannot switch if only one binding site is occupied. Do you need to specify any additional properties to turn this protein into a symport that couples the movement of solute A up its concentration gradient to the movement of solute b down its electrochemical gradient?
Gap junctions and tunneling nanotubes are two distinct types of direct intracellular communication. In comparing and contrasting gap junctions and tunneling nanotubes, which of the following statements is true? gap junctions provide a portal for small molecules, proteins and small organelles to move from cell to cell, tunneling nanotubes only permit small molecules to pass between cells typically, there are only two gap junctions that exist between adjacent cells that are communicating via this mechanism; on the other hand, there are many tunneling nanotubes between communicating cells both gap junctions and tunneling nanotubes can pass small molecules between cells none of the above is true
You are interested in the mobility of two different unknown integral plasma membrane proteins—protein X and protein Y—in a cell. In one cell, you fluorescently label all the X proteins. In another cell, you label all the Y proteins. When you perform FRAP analysis on both cells, you find that most of the protein X fluorescence has recovered within 3 minutes, but recovery of the protein Y fluorescence is significantly slower. Even after 10 minutes, only 50% of the protein Y fluorescence has recovered. Describe the FRAP experimental protocol, explain what the results tell you about mobility of the X and Y proteins, and propose a possible explanation for why the mobilities of the two proteins differ.
When the protein integrin (a transmembrane protein in human fibroblasts) is held in place, by covalent bonds to fibronectin and collagen proteins in the interstitial spaces, integrin is exhibiting: restricted movement in the membrane, based on confinement by diffusion barriers restricted movement in the membrane, based on tethering to extracellular molecules restricted movement in the membrane, based on attachment to other cells restricted movement in the membrane, based on anchoring to intracellular proteins unrestricted movement in the membrane, similar to membrane lipids