One of the most important things to consider when planning a gel is in sds page...
One of the most important things to consider when planning a gel is in sds page electrophoresis is:
volume of running buffer
mass of sample loaded
volume of sample loaded
none of the above
Homework Answers
Mass of sample loaded because small protein don't bind with sds well and it's very difficult to resolve small proteins
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One of the most important things to consider when planning a gel
is in sds page...
SDS Page Gel: The provided standard protein sample for electrophoresis consists of 9 polypeptides with molecular...
SDS Page Gel:
The provided standard protein sample for electrophoresis
consists of 9 polypeptides with molecular weights ranging from 250
to 15 KDa.
Sample 1: Protein A in a sample buffer with
B-Mercaptoethanol
Sample 2: Protein A in a sample buffer without
B-Mercaptoethanol
Sample 3: Protein B in a sample buffer with
B-Mercaptoethanol
Sample 4: Protein C in a sample buffer without
B-Mercaptoethanol
Use the picture below & the information about the proteins
above to answer the following questions.
1a....
In the nuclease digestion experiment, the scientists use a technique called gel electrophoresis. While this is...
In the nuclease digestion experiment, the scientists use a technique called gel electrophoresis. While this is related to SDS-PAGE used in the separation of membrane proteins, it is NOT THE SAME thing. From the list below, choose all the ways that gel electrophoresis is done for nuclease digestion is different from the gel electrophoresis in SDS-PAGE. Group of answer choices 1.Used to separate DNA or RNA. 2.Used to separate proteins. 3.Prteins and DNA must be separated prior to running the...
parts a,b, c please 3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the...
parts a,b, c please
3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the SDS polyacrylamide gel, you realize that instead of 2 ml, you used 4 ml of 30% acrylamide/bisacrylamide solution for the preparation of the separating gel (in both cases for 5 ml, total gel volume). How would this affect the separation of your proteins during SDS PAGE? Explain your answer! b. You have to remake the gel and are now making sure just to add...
A student tried to run an SDS PAGE gel for protein separation in a lysate. He accidently used the...
A student tried to run an SDS PAGE gel for protein separation in a lysate. He accidently used the Tris, pH8.8, buffer for the stacking gel, and the Tris, pH6.8, buffer for the resolving gel. A. What would the protein bands look like when they reach the end of stacking gel, why? B. What would the protein bands like when they finish the SDS PAGE, why? C. If the student mistakenly used Tris, pH6.8, buffer for both stacking and resolving...
Sodium dodecylsulfate (SDS) plays an important role in SDS PAGE. Select each correct description of what...
Sodium dodecylsulfate (SDS) plays an important role in SDS PAGE. Select each correct description of what SDS does in denatured electrophoresis. Choose one or more: A. Because SDS is a detergent, it supports the native state by interacting with the nonpolar portions of a protein, stabilizing the three-dimensional structure of a protein. B. SDS is an amphipathic compound that binds to the hydrophobic portion of the protein, coating the mixture and giving the protein an overall negative charge proportional to...
Carl has just finished purifying a protein and analysis by gel filtration indicated that the molecular...
Carl has just finished purifying a protein and analysis by gel filtration indicated that the molecular weight of the native (undenatured) protein was 130,000 dalton. His advisor wanted him to determine whether this protein had quaternary structure using gel electrophoresis. He wants to be able to describe the molecular weight of each of the subunits and the forces involved in linking these subunits together (disulfide linkages and/or electrostatic, hydrogen bonding and hydrophobic interactions). Carl first analyzed his pure protein sample...
A scientist subjects the mixture to denaturing Electrophoresis (SDS-PAGE) but forgets to include -mercaptoethanol in the...
A scientist subjects the mixture to denaturing Electrophoresis (SDS-PAGE) but forgets to include -mercaptoethanol in the sample buffer. The Coomassie-stained gel has only three bands as seen at right. a) Identify each sample band by labeling with the appropriate letters b)Provide an explanation for i) The number of bands ii) The apparent molecular weight indicated by the band mobilities
You start running an SDS-PAGE gel at 200V. After 10 minutes, you notice that the dye...
You start running an SDS-PAGE gel at 200V. After 10 minutes, you notice that the dye front has not moved very far and the current has dropped to almost zero. What's the most likely explanation for what has happened here?
1. Figure I shows an SDS-PAGE gel. A) Rank the 3 proteins by size, from largest...
1. Figure I shows an SDS-PAGE gel. A) Rank the 3 proteins by size, from largest to smallest. Explain why this trend is observed in SDS-PAGE gels. B) What is the purpose of SDS in SDS-PAGE? C) Sample L is the ladder. What is its purpose? D) Typically, PA (polyacrylamide) is used as the gel for protein electrophoresis, whereas agarose is used for DNA electrophoresis. Explain why a different gel material is used, Specifically referring to the pore size of...
You find yourself setting up another Western blot, however. today you are preparing the samples t...
You find yourself setting up another Western blot, however. today you are preparing the samples to load onto the SDS-PAGE gel. You are using a 4-20%SDS-PAGE gel that can hold a maximum of 30 μしper 1 You remember from you so decided to prepare each sample with a final volume of 25 uL. However, no one is perfect at pipetting, so make sure each sample is made at 1.5X the total volume needed per well. The protein you are interested...
SDS Page Gel:
The provided standard protein sample for electrophoresis
consists of 9 polypeptides with molecular weights ranging from 250
to 15 KDa.
Sample 1: Protein A in a sample buffer with
B-Mercaptoethanol
Sample 2: Protein A in a sample buffer without
B-Mercaptoethanol
Sample 3: Protein B in a sample buffer with
B-Mercaptoethanol
Sample 4: Protein C in a sample buffer without
B-Mercaptoethanol
Use the picture below & the information about the proteins
above to answer the following questions.
1a....
parts a,b, c please
3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the SDS polyacrylamide gel, you realize that instead of 2 ml, you used 4 ml of 30% acrylamide/bisacrylamide solution for the preparation of the separating gel (in both cases for 5 ml, total gel volume). How would this affect the separation of your proteins during SDS PAGE? Explain your answer! b. You have to remake the gel and are now making sure just to add...
A student tried to run an SDS PAGE gel for protein separation in a lysate. He accidently used the Tris, pH8.8, buffer for the stacking gel, and the Tris, pH6.8, buffer for the resolving gel. A. What would the protein bands look like when they reach the end of stacking gel, why? B. What would the protein bands like when they finish the SDS PAGE, why? C. If the student mistakenly used Tris, pH6.8, buffer for both stacking and resolving...
Sodium dodecylsulfate (SDS) plays an important role in SDS PAGE. Select each correct description of what SDS does in denatured electrophoresis. Choose one or more: A. Because SDS is a detergent, it supports the native state by interacting with the nonpolar portions of a protein, stabilizing the three-dimensional structure of a protein. B. SDS is an amphipathic compound that binds to the hydrophobic portion of the protein, coating the mixture and giving the protein an overall negative charge proportional to...
A scientist subjects the mixture to denaturing Electrophoresis (SDS-PAGE) but forgets to include -mercaptoethanol in the sample buffer. The Coomassie-stained gel has only three bands as seen at right. a) Identify each sample band by labeling with the appropriate letters b)Provide an explanation for i) The number of bands ii) The apparent molecular weight indicated by the band mobilities
1. Figure I shows an SDS-PAGE gel. A) Rank the 3 proteins by size, from largest to smallest. Explain why this trend is observed in SDS-PAGE gels. B) What is the purpose of SDS in SDS-PAGE? C) Sample L is the ladder. What is its purpose? D) Typically, PA (polyacrylamide) is used as the gel for protein electrophoresis, whereas agarose is used for DNA electrophoresis. Explain why a different gel material is used, Specifically referring to the pore size of...
You find yourself setting up another Western blot, however. today you are preparing the samples to load onto the SDS-PAGE gel. You are using a 4-20%SDS-PAGE gel that can hold a maximum of 30 μしper 1 You remember from you so decided to prepare each sample with a final volume of 25 uL. However, no one is perfect at pipetting, so make sure each sample is made at 1.5X the total volume needed per well. The protein you are interested...
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