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?
Homework Answers
1) SDS-PAGE are used to separate the protein on the basis of their size. protein which are larger in size move slowly as compared to those which are smaller in size.
SDS-PAGE is different from the native -PAGE because in SDS -PAGE boiling occur to denature the protein . boiling is not required in native PAGE.
2) SDS is used to provide the uniform negative charge on the protein so that the protein separated on the basis of the size and not charge because charge is same on the protein due to SDS use.
3)TEMED is added in the last because it act as a radical stabilzer and help in polymeration by stabilizing the bispolyacrylamide . TEMED accelerate the polymerisation process hence added in the last.
Add Answer to:
1-Define SDS-PAGE?
2-Explain why we use SDS (sodium dodecyl sulfate) in
electrophoresis technique to separate proteins...
parts a,b, c please 3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the...
parts a,b, c please
3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the SDS polyacrylamide gel, you realize that instead of 2 ml, you used 4 ml of 30% acrylamide/bisacrylamide solution for the preparation of the separating gel (in both cases for 5 ml, total gel volume). How would this affect the separation of your proteins during SDS PAGE? Explain your answer! b. You have to remake the gel and are now making sure just to add...
QUESTION 15 What is the purpose of adding sodium dodecyl sulfate (SDS) to the protein mixture...
QUESTION 15 What is the purpose of adding sodium dodecyl sulfate (SDS) to the protein mixture when running polyacrylamide gel electrophoresis? it induces transcription Oit denatures the proteins into a linear structure it labels the protein with a black color so it can be viewed after the it migrates through the gel O it catabolizes the protein into individual amino acids
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...
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...
Question 4-12 points Biologists use gel electrophoresis to sont DNA segments by size. DNA segments are...
Question 4-12 points Biologists use gel electrophoresis to sont DNA segments by size. DNA segments are placed at one end of a gel. DNA is negatively chargod (with a charge of two electrons per base pair). When you "run the gel" you are generating an electric field by connecting anodes and cathodes at the ends of the gel This causes the negatively charged DNA segments to move towards the positive electrode. After nunning the gel, smaller DNA segments have moved...
Biologists use gel electrophoresis to sort DNA segments by size. DNA segments are placed at one...
Biologists use gel electrophoresis to sort DNA segments by size. DNA segments are placed at one end of a gel. DNA is negatively charged (with a charge of two electrons per base pair). When you “run the gel” you are generating an electric field by connecting anodes and cathodes at the ends of the gel. This causes the negatively charged DNA segments to move towards the positive electrode. After running the gel, smaller DNA segments have moved farther from the...
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NaBH4(Sodium Borohydride) Reduction of Ketone (Organic Chemistry Lab) Questions 1. Explain the...
NaBH4(Sodium Borohydride) Reduction of Ketone (Organic
Chemistry Lab)
Questions
1.
Explain the reaction mechanism and why each reagent was used.
2. Explain the need for 2 different drying agents
3. Use
IR stretches and melting point determination to explain your
results.
4.
Report sources of error.
Experiment Procedure
Assemble the reaction apparatus as shown in Figure 14.2a,
consisting of a 3.0 mL conical vial charged with 4-t-
butylcyclohexanone (amount calculated in pre-lab) and methanol (100
μL). Attach the air condenser...
1. State and explain the definition of big-O. 2. Explain why we use big-O to compare...
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Would the methylene chloride layer be above or below the experiment? Justify your answer. 1. aqueous layer in today...
Would the methylene chloride layer be above or below the experiment? Justify your answer. 1. aqueous layer in today's ium carbonate used in the isolation of caffeine? Be specific as to the 2. Why is potass chemical species the carbonate may act on. Why was sodium sulfate used? 3. 4. After introducing 1.0 g of potassium carbonate into the centri hot water extract, it was capped, shaken, and then cooled to room temperature. Following this, roug minute. Why wasn't the...
parts a,b, c please
3. Sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis a. After pouring the SDS polyacrylamide gel, you realize that instead of 2 ml, you used 4 ml of 30% acrylamide/bisacrylamide solution for the preparation of the separating gel (in both cases for 5 ml, total gel volume). How would this affect the separation of your proteins during SDS PAGE? Explain your answer! b. You have to remake the gel and are now making sure just to add...
QUESTION 15 What is the purpose of adding sodium dodecyl sulfate (SDS) to the protein mixture when running polyacrylamide gel electrophoresis? it induces transcription Oit denatures the proteins into a linear structure it labels the protein with a black color so it can be viewed after the it migrates through the gel O it catabolizes the protein into individual amino acids
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...
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...
Question 4-12 points Biologists use gel electrophoresis to sont DNA segments by size. DNA segments are placed at one end of a gel. DNA is negatively chargod (with a charge of two electrons per base pair). When you "run the gel" you are generating an electric field by connecting anodes and cathodes at the ends of the gel This causes the negatively charged DNA segments to move towards the positive electrode. After nunning the gel, smaller DNA segments have moved...
NaBH4(Sodium Borohydride) Reduction of Ketone (Organic
Chemistry Lab)
Questions
1.
Explain the reaction mechanism and why each reagent was used.
2. Explain the need for 2 different drying agents
3. Use
IR stretches and melting point determination to explain your
results.
4.
Report sources of error.
Experiment Procedure
Assemble the reaction apparatus as shown in Figure 14.2a,
consisting of a 3.0 mL conical vial charged with 4-t-
butylcyclohexanone (amount calculated in pre-lab) and methanol (100
μL). Attach the air condenser...
Would the methylene chloride layer be above or below the experiment? Justify your answer. 1. aqueous layer in today's ium carbonate used in the isolation of caffeine? Be specific as to the 2. Why is potass chemical species the carbonate may act on. Why was sodium sulfate used? 3. 4. After introducing 1.0 g of potassium carbonate into the centri hot water extract, it was capped, shaken, and then cooled to room temperature. Following this, roug minute. Why wasn't the...
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