Question

50. Sodium dodecyl sulfate (SDS) and Triton X-100 are both detergents that can be used to lyse cells.

A. If the the goal is to study the activity of membrane proteins after cell lysis, explain why SDS would not be a good choice.
B. How does Triton X-100 work in cell lysis, and why is it a better choice of detergent to help you extract proteins?

Answer 1

SDS denatures proteins and masks their native charges, making it a poor choice for studying membrane protein activity after cell lysis. Triton X-100, on the other hand, solubilizes the lipid bilayer of cell membranes and preserves the native structure and function of proteins, making it a better choice for protein extraction.

Step-by-step explanation:

SDS is not a good choice for studying membrane protein activity after cell lysis because it denatures proteins and masks their native charges, making them uniformly negatively charged. This can disrupt the structure and function of membrane proteins, leading to inaccurate results. Triton X-100, on the other hand, works by forming micelles that solubilize the lipid bilayer of cell membranes, allowing for the extraction of membrane proteins without denaturing them. It is a better choice of detergent for extracting proteins as it preserves their native structure and function.