
An unknown protein migrates between markers of 50,000 and 40,000 Da on an SDS-PAGE gel. What is the estimated molecular weight of the unknown protein?
How does SDS-PAGE separate protein subunits without cleaving disulfide bonds?
Why are molecular weight markers important in SDS-PAGE?
What is the significance of the linear relationship between the log of molecular weight and relative migration in SDS-PAGE?
How does SDS-PAGE handle proteins with quaternary structures?
How does SDS ensure proteins separate based solely on mass in SDS-PAGE?
Which lane in an SDS-PAGE gel would indicate the most effective protein purification technique?