Life: The Science of Biology
11th Edition
ISBN: 9781319010164
Author: David E. Sadava, David M. Hillis, H. Craig Heller, Sally D. Hacker
Publisher: W. H. Freeman
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Chapter 5, Problem 4Q
Summary Introduction
To review:
The method to use fluorescent tagging to track two different proteins at the same time.
Introduction:
The green fluorescent protein (GFP) is a protein that fluoresces and is obtained from the aquatic animal called jellyfish, having the scientific name Aequorea victoria. It is made up of 238 amino acids. It emits green fluorescent light in the presence of ultraviolet light.
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Life: The Science of Biology
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- Mild detergents, like Triton X-100, would be the best for isolation of peripheral proteins from the plasma membrane (without denaturing these proteins) because: they are non-polar with mostly negatively-charged regions they are non-polar with mostly positively-charged regions they are non-polar with mostly uncharged regions they are polar with mostly uncharged regions they are polar with mostly charged regionsarrow_forwardHow transfer of information occurs (nucleicacid is decoded into a protein) ?arrow_forwardWhat type of DNA structure is recognized by RecG and RuvABC?Do you think these proteins recognize DNA sequences? Be specificabout what type(s) of molecular recognition these proteins canperform.arrow_forward
- Two proteins bind the same ligand, and the data is shown below. Select the best answer based on this data: Protein A binds the ligand with higher affinity, as it has the highest KD value Protein B binds the ligand with higher affinity, as it has the lowest KD value Protein B binds the ligand with higher affinity, as it has the highest KD value Protein A binds the ligand with higher affinity, as it has the lowest KD valuearrow_forwardDiscuss and present the Green Fluorescent Protein?arrow_forwardHow do cells respond to tinygradients of molecules in theirenvironment, as required for knowingtheir positions? How are morphogengradients reliably interpreted?arrow_forward
- Under the microscope, the fluorescent signal from an isolated quantum point will form a stain: A.Approximately the same size as a fluorescent protein of the same colourB.Much smaller than a fluorescent protein, regardless of colourC.Relatively dark compared to antibodyD.Which corresponds approximately to the size of the quantum point, 20 to 40nm.arrow_forwardWhat is the advantage of using a TEM instead of an LM to study intracellular structure?arrow_forwardDefine denaturation and give some examples of agents that cause denaturation.arrow_forward
- Which of the following experiments can be used to determine the localization of a protein in living cells? a. Isoelectric Focusing gel electrophoresis b. Mass spectroscopy of a MALDI-ionized protein c. X-ray Crystallography of a protein d. NMR study of a 15N-labeled protein e. Confocal microscopy study of a GFP-tagged proteinarrow_forwardYou are using fluorescence microscopy to study a plasma membrane protein that is fused to green fluorescent protein (GFP). Adding GFP to a protein allows us to monitor the protein in live cells using light microscopy without the need for any special stains. Under baseline conditions, the fusion protein is evenly distributed over the surface of the cell. You use the microscope software and laser to photobleach an ROI and watch for the recovery of fluorescence in real time. you have a control protein, a GFP fusion with the insulin receptor, where the ROI fully recovers from photobleaching in 10 min. However, when Protein X is fused with GFP, the fluorescence recovers only to 10% the starting levels in 10 min in the same cell type under the same experimental conditions. Provide two different, reasonable explanations for the different results with these two fusion proteins.arrow_forwardYou 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.arrow_forward
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