Electrophoresis is not used for the separation of
Q. Electrophoresis is not used for the separation of ________. Nucleic acids Proteins Amino acids Lipids Answer: Lipids
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Electrophoresis MCQs
The ratio of velocity (‘v’) of biomolecule in a medium under constant electric field (‘E’) is called ‘Electrophoretic mobility’ denoted as ‘µ’. ‘µ’ is mathematically expressed as
Q. The ratio of velocity (‘v’) of biomolecule in a medium under constant electric field (‘E’) is called ‘Electrophoretic mobility’ denoted as ‘µ’. ‘µ’ is mathematically expressed as: µ = E/v µ = 1/(Ev) µ = VE µ = v/E Answer: µ = v/E
Function of β-mercaptoethanol in SDS-PAGE is
Q. Function of β-mercaptoethanol in SDS-PAGE is__________. To give negative charges to amino acids in the proteins For the oxidation of disulfide bonds in the proteins For breaking hydrogen bonds in the proteins For the reduction of disulfide bonds in the proteins Answer: For the reduction of disulfide bonds in the proteins
In electrophoresis, the electrophoretic mobility (‘µ’) is determines the characteristics of migration of different biomolecules. Which of the following is not having any influence in ‘µ’?
Q. In electrophoresis, the electrophoretic mobility (‘µ’) is determines the characteristics of migration of different biomolecules. Which of the following is not having any influence in ‘µ’? Size of molecule Shape of molecule Molecular weight Stereochemistry of molecule Answer: Stereochemistry of molecule
In native-PAGE the separation of protein is influenced by
Q. In native-PAGE the separation of protein is influenced by ___________. Charge of protein Size of protein pI of protein Both (a) and (b) Answer: Both (a) and (b)
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The role of urea in PAGE separation of DNA is to
Q. The role of urea in PAGE separation of DNA is to _______. Act as anion Act as cation Helps to denature the DNA Provide buffer stability of the gel Answer: Helps to denature the DNA
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In a native PAGE, proteins are separated on the basis of
Q. In a native PAGE, proteins are separated on the basis of net negative charge net charge and size net positive charges size net positive charge Answer: net charge and size
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In an SDS-PAGE
Q. In an SDS-PAGE proteins are denatured by the SDS proteins have the same charge-to-mass ratio smaller proteins migrate more rapidly through the gel all of the above Answer: all of the above
In SDS-PAGE, the protein sample is first
Q. In SDS-PAGE, the protein sample is first treated with a reducing agent and then with anionic detergent followed by fractionation by electrophoresis fractionated by electrophoresis then treated with an oxidizing agent followed by anionic detergent treated with a oxidizing agent and then with anionic detergent followed by fractionation by electrophoresis none of the above
In isoelectric focusing, proteins are separated on the basis of their
Q. In isoelectric focusing, proteins are separated on the basis of their relative content of positively charged residue only relative content of negatively charged residue only size relative content of positively and negatively charged residue Answer: relative content of positively and negatively charged residue
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