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1) If PAGE is carried out after subjecting the sample to SDS and beta-mercaptoethanol, then proteins will be separated on the basis of:

a) Mass
b) Native charge
c) Sequence
d) Shape

1 Answer

1 vote

Final answer:

Proteins are separated on the basis of mass during SDS-PAGE after treatment with SDS and beta-mercaptoethanol, as these agents denature proteins and negate their native charges. The correct option is a) Mass

Step-by-step explanation:

When polyacrylamide gel electrophoresis (PAGE) is carried out after subjecting a sample to SDS (sodium dodecyl sulfate) and beta-mercaptoethanol, proteins will be separated on the basis of their mass.

SDS functions as a detergent that denatures proteins, ensuring they are uniformly coated with a negative charge and thus masking their native charge. Beta-mercaptoethanol is used to reduce disulfide bonds to further ensure denaturation.

As a result, during SDS-PAGE, the only factor affecting protein migration through the gel is the molecular weight (or mass) of the protein, as proteins are forced to migrate through a polyacrylamide matrix under an electric field, with smaller proteins moving faster and further than larger ones. The correct option is a) Mass

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