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?
Homework Answers
In denaturing gel electrophoresis there is single band of 100kDa which means this protein is made up of three subunit of identical subunit of 100kDa so 100x3= 300kDa.
Here in denaturing gel electrophoresis, we used SDS page which cause breakage of non-covelent bond so all subunit become seperated from each other.
In non-denaturing gel, there is single band of 300kDa as in this gel SDS is absent and hence weak interection between subunits are present so formed 300kDa single complex protein.
Charge-by-mass ratio is commonly used for seperation in case of horizontal gel electrophoresis like DNA or RNA
.hope it's clear..thanks
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If a protein is a homotrimer with a molecular weight of 300 kDa,
at what molecular...
A purified protein has a molecular mass of 360 kDa when measured by size exclusion chromatography....
A purified protein has a molecular mass of 360 kDa when measured by size exclusion chromatography. When analyzed by gel electrophoresis in the presence of SDS, three bands are observed, with molecular masses of 160, 140, and 60 kDa. When gel electrophoresis is carried out in the presence of SDS and dithiothreitol three bands are once again observed, with molecular masses of 140, 80, and 60 kDa. What is the subunit composition of the protein?
A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein,...
A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein, Y. Protein X is composed of two polypeptide chains linked by disulfide bonds. Protein Y is composed of three polypeptide chains linked by disulfide bonds. The complex is analyzed by native PAGE, reducing SDS-PAGE and non-reducing SDS-PAGE. Native PAGE does not include sodium dodecyl sulfate, or SDS. Reducing SDS-PAGE uses both SDS and a reducing agent in the buffer. Non-reducing SDS-PAGE uses SDS, but...
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?
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel...
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel filtration chromatography. The SDS-polyacrylamide gel electrophoresis (SDS PAGE) of the protein yields a single band corresponding to molecular weight of 70,000 Dalton. However, in the presence of the reducing agent, B-mercaptoethanol, the SDS PAGE shows two bands, corresponding to molecular weights of 30,000 and 20,000 Dalton. unspecified protein, at physiological conditions, is 70,000 ure a. From these data, describe the native protein in terms...
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....
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...
Chapter 3 Home Active and Due Dates Chapter Homework Resouros Ghve Up! Feedback PAGE A protein...
Chapter 3 Home Active and Due Dates Chapter Homework Resouros Ghve Up! Feedback PAGE A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein, Y. Protein X is composed two polypeptide chains linked by disulfide bonds. Protein Y is composed of three polypeptide chain linked by disulfide bonds The complex is analyzed by native PAGE, reducing SDS-PAGE and non-reducing SDS-PAGE Native PAGE does not include sodium dodecyl sulfate, or SDS. Reducing SDS-PAGE uses both...
What separation method commonly uses a horizontal gel electrophoresis apparatus? Why?
What separation method commonly uses a horizontal gel electrophoresis apparatus? Why?
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...
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?
A purified protein has a molecular mass of 360 kDa when measured by size exclusion chromatography. When analyzed by gel electrophoresis in the presence of SDS, three bands are observed, with molecular masses of 160, 140, and 60 kDa. When gel electrophoresis is carried out in the presence of SDS and dithiothreitol three bands are once again observed, with molecular masses of 140, 80, and 60 kDa. What is the subunit composition of the protein?
A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein, Y. Protein X is composed of two polypeptide chains linked by disulfide bonds. Protein Y is composed of three polypeptide chains linked by disulfide bonds. The complex is analyzed by native PAGE, reducing SDS-PAGE and non-reducing SDS-PAGE. Native PAGE does not include sodium dodecyl sulfate, or SDS. Reducing SDS-PAGE uses both SDS and a reducing agent in the buffer. Non-reducing SDS-PAGE uses SDS, but...
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?
4. The molecular weight of an Dalton, as determined by sedimentation equilibrium measurements and by gel filtration chromatography. The SDS-polyacrylamide gel electrophoresis (SDS PAGE) of the protein yields a single band corresponding to molecular weight of 70,000 Dalton. However, in the presence of the reducing agent, B-mercaptoethanol, the SDS PAGE shows two bands, corresponding to molecular weights of 30,000 and 20,000 Dalton. unspecified protein, at physiological conditions, is 70,000 ure a. From these data, describe the native protein in terms...
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....
Chapter 3 Home Active and Due Dates Chapter Homework Resouros Ghve Up! Feedback PAGE A protein sample complex consists of two proteins, a smaller protein, X, and a larger protein, Y. Protein X is composed two polypeptide chains linked by disulfide bonds. Protein Y is composed of three polypeptide chain linked by disulfide bonds The complex is analyzed by native PAGE, reducing SDS-PAGE and non-reducing SDS-PAGE Native PAGE does not include sodium dodecyl sulfate, or SDS. Reducing SDS-PAGE uses both...
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...
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