1. When using SDS-PAGE, proteins will be separated on the basis of what physical property? 2. ...
1. When using SDS-PAGE, proteins will be separated on the basis of what physical property?
2. You are given two proteins, one with a molecular weight of 67,435 Daltons and other with a molecular weight of 21,345 Daltons. Which protein will move further in the SDS-PAGE?
Homework Answers
1. SDS-PAGE is a gel electrophoresis method of separating protein fragments on the basis of molecular weight. SDS (Sodium dodecyl sulfate) is a detergent that denatures the protein and imparts uniform negative charge to all the protein molecules so that the separation of protein fragments take place solely on the basis of the mass.
2. Proteins with low molecular weight move faster in SDS PAGE. So the protein with molecular weight 21,345 Daltons will move further in the SDS PAGE as compare to the protein with molecular weight 67,435 Daltons.
Add Answer to:
1. When using SDS-PAGE, proteins will be separated on the basis
of what physical property?
2. ...
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...
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...
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....
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...
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 is often used to determine the location and orientation of membrane associated proteins. Commonly, experimental...
SDS-PAGE is often used to determine the location and orientation of membrane associated proteins. Commonly, experimental preparations of membranes are treated in a variety of ways in order to extract the proteins, which are then subjected to SDS-PAGE. These treatments will affect membrane proteins in different ways, based on how they are arranged in the membrane. One of the most common pre-treatments is by the digestive enzyme trypsin, which degrades polypeptide chains. Trypsin is too large to cross a membrane,...
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.
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...
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?
1-Define SDS-PAGE? 2-Explain why we use SDS (sodium dodecyl sulfate) in electrophoresis technique to separate proteins...
1-Define SDS-PAGE? 2-Explain why we use SDS (sodium dodecyl sulfate) in electrophoresis technique to separate proteins or nucleic acids? 3- Explain why TEMED should be the last reagent that add to the solution when preparing the gel?
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...
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...
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....
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...
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 is often used to determine the location and orientation of membrane associated proteins. Commonly, experimental preparations of membranes are treated in a variety of ways in order to extract the proteins, which are then subjected to SDS-PAGE. These treatments will affect membrane proteins in different ways, based on how they are arranged in the membrane. One of the most common pre-treatments is by the digestive enzyme trypsin, which degrades polypeptide chains. Trypsin is too large to cross a membrane,...
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...
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?
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