Question

Sodium dodecylsulfate (SDS) plays an important role in SDS PAGE. Select each correct description of what SDS does in denatured electrophoresis. Choose one or more: A. Because SDS is a detergent, it supports the native state by interacting with the nonpolar portions of a protein, stabilizing the three-dimensional structure of a protein. B. SDS is an amphipathic compound that binds to the hydrophobic portion of the protein, coating the mixture and giving the protein an overall negative charge proportional to the size of the protein. C. SDS is a charged detergent that neutralizes the protein, allowing the protein to migrate through the gel based on size. D. Because SDS is a detergent, it plays a role in denaturing the protein.

Answer 1

SDS is an anionic detergent it denatures the protein, the hydrophobic chain of the SDS interacts with the protein and the protein becomes negatively charged, the proteins are separated on the acrylamide gel based on the size of the protein.

so the answers are

B) SDS is an amphipathic compound that binds to the hydrophobic portion of the protein, coating mixture and giving the protein an overall negative charge proportional to the size of the protein.

D) because SDS is a detergent, it plays a role in denaturing the protein.