If a sample contained a protein homotetramer and was placed on a denaturing SDS PAGE for...
If a sample contained a protein homotetramer and was placed on a denaturing SDS PAGE for separation, how many bands would you expect to appear?
Homework Answers
Solution-A simgle band eould appear in this scenario as the protein has four units but they are same so there will be no movement with respect to mass, size or charge. A single thick band would appear.
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If a sample contained a protein homotetramer and was placed on a
denaturing SDS PAGE for...
"You have run both non-denaturing and denaturing samples of your purified fluorescent protein on the SDS-PAGE...
"You have run both non-denaturing and denaturing samples of your purified fluorescent protein on the SDS-PAGE gel. When do you expect to see a difference between the two samples? Briefly explain." Hey!! if anyone could help me with this question I would greatly appreciate it. It is based on my cell bio lab and I don't understand the question. Thankyou in advance!!
If a protein is a homotrimer with a molecular weight of 300 kDa, at what molecular...
If a protein is a homotrimer with a molecular weight of 300 kDa, at what molecular weight(s) would you expect to see bands using denaturing SDS-PAGE? Non-denaturing elec-trophoresis? What separation method commonly uses a horizontal gel electrophoresis apparatus? Why?
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
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...
5. A native protein has a molecular weight of 150,000 Da. Denaturing SDS electrophoresis results in...
5. A native protein has a molecular weight of 150,000 Da. Denaturing SDS electrophoresis results in two bands with molecular weights of approximately 53,000 and 23,000 Da. What arrangement of polypeptide chains in the native protein would best explain these results? 2. If two proteins have the same molecular weight, are they necessarily the same protein? Can you definitely assign the identity of a protein based on its molecular weight? Why or why not?
After performing SDS-PAGE of a protein extract, there will be a number of protein “bands” in...
After performing SDS-PAGE of a protein extract, there will be a number of protein “bands” in a lane of the gel. In a single “band” all proteins have the same A.native (i.e. original) charge B. function C. molecular mass
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....
A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment with 2-mercaptoethanol...
A protein gives two bands of 50 and 80 kD on SDS PAGE. Treatment with 2-mercaptoethanol gives two bands of 50kD and 40kD. Give detailed information about this protein including its molecular weight.
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...
Select the true statements about SDS-PAGE, a method of separating proteins. Assume that SDS-PAGE is performed...
Select the true statements about SDS-PAGE, a method of separating proteins. Assume that SDS-PAGE is performed under reducing conditions. Proteins are separated in a polyacrylamide gel matrix. Sodium dodecyl sulfate binds proteins, resulting in protein-SDS complexes that are similar in size. Protein-SDS complexes migrate toward the negative electrode. Smaller proteins migrate faster through the polyacrylamide gel. Proteins are visualized using a dye that binds to the gel matrix, but not to proteins. Protein-SDS complexes have similar mass to charge ratios;...
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
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...
5. A native protein has a molecular weight of 150,000 Da. Denaturing SDS electrophoresis results in two bands with molecular weights of approximately 53,000 and 23,000 Da. What arrangement of polypeptide chains in the native protein would best explain these results? 2. If two proteins have the same molecular weight, are they necessarily the same protein? Can you definitely assign the identity of a protein based on its molecular weight? Why or why not?
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....
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...
Select the true statements about SDS-PAGE, a method of separating proteins. Assume that SDS-PAGE is performed under reducing conditions. Proteins are separated in a polyacrylamide gel matrix. Sodium dodecyl sulfate binds proteins, resulting in protein-SDS complexes that are similar in size. Protein-SDS complexes migrate toward the negative electrode. Smaller proteins migrate faster through the polyacrylamide gel. Proteins are visualized using a dye that binds to the gel matrix, but not to proteins. Protein-SDS complexes have similar mass to charge ratios;...
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