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
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After performing SDS-PAGE of a protein extract, there will be a
number of protein “bands” in...
Predict the patterns (number of bands and apparent molecular weights) of the following proteins on SDS...
Predict the patterns (number of bands and apparent molecular weights) of the following proteins on SDS gels: a. A monomeric protein with a molecular weight of 35,000 Da b. A trimetric protein containing three chains, each with a molecular weight of 60,000 Da c. Immunoglobulin G (Nelson and Cox, page 178) in a non-reducing gel (no beta -mercaptoethanol added in the sample solution) - the light chains have a molecular weight of 25,000 Da and the heavy chains 50,000 Da...
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...
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;...
The next question concerns the SDS-PAGE figure below. Lane 1 contains an unknown sample. Lane M...
The next question concerns the SDS-PAGE figure below. Lane 1 contains an unknown sample. Lane M contains a mixture of the following proteins (listed alphabetically). M 1 P1 - - Protein Bovine carbonic anhydrase Bovine milk aprotinin Bovine milk lactalbumin Bovine serum albumin Beta-galactosidase Chicken egg ovalbumin Rabbit muscle myosin Soybean trypsin inhibitor Molecular Mass 29,000 6,500 14,200 66,000 116,000 45,000 205,000 20,000 - - P3 - P4 L 19. The wild type (normal) human B-chain hemoglobin protein has a...
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...
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....
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...
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.
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...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
Predict the patterns (number of bands and apparent molecular weights) of the following proteins on SDS gels: a. A monomeric protein with a molecular weight of 35,000 Da b. A trimetric protein containing three chains, each with a molecular weight of 60,000 Da c. Immunoglobulin G (Nelson and Cox, page 178) in a non-reducing gel (no beta -mercaptoethanol added in the sample solution) - the light chains have a molecular weight of 25,000 Da and the heavy chains 50,000 Da...
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...
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;...
The next question concerns the SDS-PAGE figure below. Lane 1 contains an unknown sample. Lane M contains a mixture of the following proteins (listed alphabetically). M 1 P1 - - Protein Bovine carbonic anhydrase Bovine milk aprotinin Bovine milk lactalbumin Bovine serum albumin Beta-galactosidase Chicken egg ovalbumin Rabbit muscle myosin Soybean trypsin inhibitor Molecular Mass 29,000 6,500 14,200 66,000 116,000 45,000 205,000 20,000 - - P3 - P4 L 19. The wild type (normal) human B-chain hemoglobin protein has a...
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...
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....
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...
Why are proteins heat denatured prior to analysis in SDS-PAGE? Select all answers that apply. Denaturation of the protein is necessary so that proteins run proportionally to their size, based on the interaction of SDS with the unfolded protein. Heat is used to hydrolyze the peptide bonds of the protein. The heat step allows the proteins to unfold, enabling the protein chain to be coated with SDS molecules. Heat is used to hydrolyze disulfide bonds. QUESTION 2 1.5 points Saved...
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