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Polyacrylamide gel electrophoresis is performed for
  • a)
    to separate proteins and DNA of size less than 500 bp
  • b)
    to separate only proteins
  • c)
    to separate only DNA
  • d)
    to separate protein along with RNA
Correct answer is option 'A'. Can you explain this answer?
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Polyacrylamide gel electrophoresis is performed fora)to separate prote...
Polyacrylamide gel electrophoresis is used to separate proteins and DNA less than 500 bp.
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Polyacrylamide gel electrophoresis is performed fora)to separate prote...
Polyacrylamide gel electrophoresis (PAGE) is a widely used technique in biochemistry and molecular biology to separate biomolecules based on their size and charge. It is commonly used to separate proteins and DNA fragments.

Polyacrylamide gel electrophoresis is performed to separate proteins and DNA of size less than 500 bp. Here is a detailed explanation:

1. Principle of Polyacrylamide Gel Electrophoresis:
- Electrophoresis is a technique that uses an electric field to move charged molecules through a gel matrix.
- Polyacrylamide gel is a commonly used matrix for electrophoresis due to its uniform pore size and excellent resolution for small molecules.

2. Separation of Proteins and DNA:
- Polyacrylamide gel electrophoresis can be used to separate proteins and DNA fragments based on their size and charge.
- In the case of proteins, the separation is based on their molecular weight.
- In the case of DNA fragments, the separation is based on their base pair length.

3. Size Limitation:
- Polyacrylamide gel electrophoresis is particularly suitable for separating small molecules, such as proteins and DNA fragments less than 500 base pairs (bp) in length.
- For larger molecules, agarose gel electrophoresis is typically used.

4. Gel Preparation:
- Polyacrylamide gel is prepared by polymerizing acrylamide monomers and a crosslinking agent, usually bis-acrylamide.
- The concentration of acrylamide determines the pore size of the gel, which in turn affects the separation of biomolecules.
- Higher acrylamide concentrations result in smaller pore sizes and better resolution for smaller molecules.

5. Electrophoresis Setup:
- The polyacrylamide gel is cast between two glass plates with a comb inserted at one end to create sample wells.
- The gel is submerged in a buffer solution that provides ions for conducting electricity.

6. Loading the Samples:
- The protein or DNA samples are mixed with a loading dye, which contains a tracking dye that helps to monitor the progress of electrophoresis.
- The samples are loaded into the wells of the gel.

7. Electrophoresis:
- An electric current is applied to the gel, causing the charged molecules to migrate through the gel matrix.
- The movement of the molecules is influenced by their charge, size, and the electric field strength.
- Smaller molecules migrate faster and travel farther through the gel.

8. Visualization:
- After electrophoresis, the gel is stained with a dye that binds to proteins or DNA, making them visible.
- The stained gel can be visualized under UV light or using a colorimetric stain.

9. Analysis:
- The separated proteins or DNA fragments can be quantified and analyzed based on their migration patterns.
- The distance migrated by each band can be compared to molecular weight markers to estimate the size of the molecules.

In conclusion, polyacrylamide gel electrophoresis is performed to separate proteins and DNA fragments less than 500 base pairs in length. It is a versatile technique widely used in molecular biology and biochemistry research.
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Explanation:The separation techniques of proteins are used to isolate and purify proteins from complex mixtures. These techniques are based on various properties of proteins such as solubility, charge, size, and others. However, the technique of protein separation based on viscosity is not commonly used. Protein solubility:Protein solubility refers to the ability of a protein to dissolve in a given solvent. Different proteins have different solubilities in different solvents. This property is often used in techniques like precipitation, where proteins are selectively precipitated out of solution based on their solubility.Protein charge:Protein charge refers to the net charge of a protein molecule, which is determined by the presence of charged amino acid residues such as lysine, arginine, aspartic acid, and glutamic acid. Techniques like electrophoresis and ion exchange chromatography utilize the charge differences between proteins to separate them.Protein size:Protein size refers to the molecular weight or size of a protein molecule. Techniques such as gel filtration chromatography and SDS-PAGE separate proteins based on their size. In gel filtration chromatography, proteins are separated based on their ability to enter and pass through a porous gel matrix, while in SDS-PAGE, proteins are separated based on their migration through a gel under the influence of an electric field.Protein viscosity:Protein viscosity refers to the resistance of a protein solution to flow. While protein viscosity can vary depending on factors such as protein concentration, temperature, and pH, it is not typically used as a property for protein separation. In conclusion, the separation techniques of proteins are based on properties such as solubility, charge, and size. Protein viscosity is not commonly used as a property for protein separation.

Polyacrylamide gel electrophoresis is performed fora)to separate proteins and DNA of size less than 500 bpb)to separate only proteinsc)to separate only DNAd)to separate protein along with RNACorrect answer is option 'A'. Can you explain this answer?
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