Homework Answers
Answer: to determine protein size
Explanation:
Ladder is a set of standards that are used to identify the approximate size of a molecule run on gel during electrophoresis, Different ladders are available, protein ladder, DNA ladder and RNA ladders. Protein ladder is used in SDS-PAGE gels that allow to determine the location of protein of interest based on it molecular size.
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Why do we use a ladder in SDS-PAGE gels? to determine SDS-PAGE electrical properties to determine...
Explain the difference between SDS-PAGE gels with acrylamide to the bis-acrylamide ratio of 29:1 compared to...
Explain the difference between SDS-PAGE gels with acrylamide to the bis-acrylamide ratio of 29:1 compared to 37:1? In which one do proteins move faster and why?
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...
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...
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...
1. Although you are making 12% SDS – PAGE gels, other percentages can be made. a....
1. Although you are making 12% SDS – PAGE gels, other percentages can be made. a. When would you want to use a 10% gel? b. When would you want to use a 20% gel? 2. Why must you use both acrylamide and bis – acrylamide to make your gel? 3. There are three ratios of acrylamide:bis – acrylamide that are used when making these types of gels. a. What is the primary application for a gel made up of...
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?
Explanation of SDS-PAGE for Western blotting procedure, PLEASE answer the questions BELOW: 1. What does a...
Explanation of SDS-PAGE for Western blotting procedure, PLEASE answer the questions BELOW: 1. What does a gel electrophoresis allow you to do? 2. What is a gel? 3. How do you make the protein move, and why does this work? 4. Which protein fragments travel the furthest and why? 5. Name 3 materials used to make a gel. 6. What is polyacrylamide? 7. What is the purpose of the buffer? 8. What is the comb (in the gel) for? 9....
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before SDS-PAGE Why do SDS-coated proteins migrate in an electric field? e...
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before SDS-PAGE Why do SDS-coated proteins migrate in an electric field? e molecular mass of myosin light chain I is approximately 22 kD, myosin heavy chain is 200 kD ane actin is 42 kD, Which proteins will migrate fastest through the gel? Why?
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before...
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...
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 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...
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...
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...
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before SDS-PAGE Why do SDS-coated proteins migrate in an electric field? e molecular mass of myosin light chain I is approximately 22 kD, myosin heavy chain is 200 kD ane actin is 42 kD, Which proteins will migrate fastest through the gel? Why?
In the Western blot experiment, )Why are proteins treated with ionic detergent (SDS), reducing agents (DTT), and heat before...
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...
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....
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