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What is a key advantage of using SDS-PAGE in protein purification?
How can SDS-PAGE be used to assess the purity of a protein sample?
Which of the following statements correctly differentiates SDS-PAGE from native PAGE?
If a protein subunit has a molecular weight of 50 kDa, how would its relative mobility compare to a 25 kDa subunit in SDS-PAGE?
Which component of SDS-PAGE is responsible for denaturing proteins?
What happens to the charge of a protein as it migrates through different pH regions in an isoelectric focusing gel?
What role do ampholytes play in establishing a stable pH gradient in isoelectric focusing?
How does a linear pH gradient enhance the resolution of protein separation in isoelectric focusing?
What are the two main components of 2D electrophoresis?
What is the purpose of turning the isoelectric focusing gel 90 degrees in 2D electrophoresis?
In a 2D electrophoresis experiment, two proteins with identical isoelectric points are separated. What allows for this separation?
What is the primary purpose of diagonal electrophoresis in biochemistry?
After identifying disulfide-linked peptides using diagonal electrophoresis, what is the next step to determine the positions of disulfide bonds?
Why is diagonal electrophoresis considered a valuable tool in biochemical research?