50+ MCQs On SDS Page with Answers and FREE PDF

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MCQs On SDS Page with Answers

1. If proteins are separated according to their electrophoretic mobility then the type of electrophoresis is:

a) SDS PAGE

b) Affinity Electrophoresis

c) Electro focusing

d) Free flow electrophoresis

Answer: a

2. Which of the following statements is true about SDS polyacrylamide chromatography?

a) SDS polyacrylamide gel electrophoresis separates proteins on the basis of size

b) SDS polyacrylamide gel electrophoresis separates proteins on the basis of charge

c) SDS binds to proteins non-covalently with a stoichiometry of around one SDS molecule per three amino acids

d) SDS binds to proteins non-covalently with a stoichiometry of around one SDS molecule per one amino acid

Answer: b

3. In SDS-PAGE, protein sample is first treated with detergent sodium dodecyl sulfate (SDS), in order to

a) Make the protein become negatively charged.

b) Make the protein become positively charged.

c) Renature the protein.

d) Adjust the pH of protein.

Answer: a

4. The sample is then fractionated by electrophoresis through a _______. As all the proteins now have an _______ to mass ratio, they are separated on the basis of their _____.

a) Acrylamide solution, identical charge, mass

b) Polyacrylamide gel, identical charge, density

c) Polyacrylamide gel, identical density, mass

d) Polyacrylamide gel, identical charge, mass

Answer: d

5. What is the purpose of using bromophenol blue in the sample buffer?

a) To ionize the sample.

b) To monitor the electrophoretic run.

c) To act as standard control

d) To adjust the pH of sample.

Answer: b

6. Which the following statements is/are true about the stacking gel?

i. The stacking gel solution contains acrylamide.

ii. It is on the top of the separating gel.

iii. It is used to dilute the protein sample before it enters the main separating gel.

iv. It is into this gel that the wells are formed and the proteins loaded.

a)  i, ii and iii only.

b) ii, iii and iv only.

c) i, ii and iv only.

d) All of them.

Answer: c

7. Each band on the gel represents a different protein (or protein subunit); _____ proteins move through the gel more _____ than_____ proteins and therefore are found nearer the _____ of the gel.

a) Larger, rapidly, smaller, top

b) Smaller, rapidly, larger, bottom

c) Larger, slowly, smaller, bottom

d) Smaller, slowly, larger, bottom

Answer: b

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FAQs on SDS Page

What is SDS in chromatography?

Sodium dodecyl sulfate (SDS) is an anionic detergent and is most commonly used in protein chemistry to denature proteins and dissolve proteins and protein aggregates immersed in water, such as in SDS-PAGE.

What does SDS do to proteins?

So, what is the function of SDS in chromatography?  It denatures proteins by binding to the protein chain with its hydrocarbon tail. This accomplishes three things.

What is SDS and how does it work?

SDS is an abbreviation for sodium dodecyl sulfate. SDS is a detergent, which can dissolve proteins. Proteins are made up of amino acids linked by peptide bonds. The carboxyl groups of one amino acid are attracted to the amino group on the other end; the attraction closes the gap (disulfide bond) that holds the polypeptide backbone in shape. SDS denatures proteins by wrapping around the polypeptide backbone. By heating the protein sample between 70-100°C in the presence of excess SDS and thiol reagent, disulfide bonds are cleaved (broken) and the protein is fully dissociated into its subunits

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