Hemoglobin has a molecular weight of 65 kDa, but the SDS-PAGE band shows up lower. Explain.
Hemoglobin has a molecular weight of 65 kDa, but the SDS-PAGE band shows up lower. Explain.
Homework Answers
The lower band may be due to proteolytic cleavage and the hemoglobin may undergoes post-translational modification, such as phosphorylation or glycosylation, resulting in differential mobilities on SDS-PAGE.as a results it shows lower SDS-PAGE band.
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Hemoglobin has a molecular weight of 65 kDa, but the SDS-PAGE
band shows up lower. Explain.
Help please 2) The following image shows an SDS-PAGE gel: 1 2 3 4 - 5...
Help please
2) The following image shows an SDS-PAGE gel: 1 2 3 4 - 5 6 7 974 kDa 66.2 kDa 45.0 kDa 31.0 kDa 21.5 kDa 14.4 kDa Please mark the only statement that could be accurately made using this SDS-PAGE gel. A. The protein in highest concentration in lane 4 is basic. B. The protein in highest concentration in lanes 5, 6 and 7 has a molecular weight of less than 66.2 kilodaltons. C. The protein with...
1d. Finally, you run SDS-PAGE in the presence of 2-mercaptoet urun SDS-PAGE in the presence of...
1d. Finally, you run SDS-PAGE in the presence of 2-mercaptoet urun SDS-PAGE in the presence of 2.mernantoethanol on a subsample of each peak from each column in parts 1a and ic. The image below shows the migration of molecular weight markers and labels for each sample lane Indicate the location of protein band(s) for each of your samples. Identify the protein(s) in each band in each lane and explain your reasoning Anion Exchange 12 Gel Fitration 12 Gel filtation after...
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....
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...
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 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
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?
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...
please help Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE)....
please help
Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE). d) B-sheet protein structures can be stabilized by hydrogen bonding between distant residues on the same polypeptide. e) B-sheets are a type of secondary structure and are found in every protein.
If the molecular weight of Protein G:B1 is 8 kDa, what is the concentration (in mg...
If the molecular weight of Protein G:B1 is 8 kDa, what is the concentration (in mg / mL) of a solution of this protein which has an absorbance (A) =0.2 at l = 280 nm? How many grams of protein are present in 1 mL of this solution?
Help please
2) The following image shows an SDS-PAGE gel: 1 2 3 4 - 5 6 7 974 kDa 66.2 kDa 45.0 kDa 31.0 kDa 21.5 kDa 14.4 kDa Please mark the only statement that could be accurately made using this SDS-PAGE gel. A. The protein in highest concentration in lane 4 is basic. B. The protein in highest concentration in lanes 5, 6 and 7 has a molecular weight of less than 66.2 kilodaltons. C. The protein with...
1d. Finally, you run SDS-PAGE in the presence of 2-mercaptoet urun SDS-PAGE in the presence of 2.mernantoethanol on a subsample of each peak from each column in parts 1a and ic. The image below shows the migration of molecular weight markers and labels for each sample lane Indicate the location of protein band(s) for each of your samples. Identify the protein(s) in each band in each lane and explain your reasoning Anion Exchange 12 Gel Fitration 12 Gel filtation after...
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....
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...
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 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
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?
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...
please help
Tor F. A) High molecular weight proteins will migrate farther during gel electrophoresis (SDS-PAGE). d) B-sheet protein structures can be stabilized by hydrogen bonding between distant residues on the same polypeptide. e) B-sheets are a type of secondary structure and are found in every protein.
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