Difficulty: Easy
Correct Answer: All of the above
Explanation:
Introduction:
Agarose gel electrophoresis for DNA and SDS–PAGE for proteins are cornerstone techniques for separating biomolecules by size. Despite analyzing different macromolecules with different gel matrices, they share several core physical principles. This question asks you to identify the commonalities that make these methods conceptually similar in the lab.
Given Data / Assumptions:
Concept / Approach:
Both assays separate primarily by size because the charge-to-mass ratio is roughly constant across species being compared. DNA is inherently uniformly charged; proteins become uniformly charged after SDS binding and denaturation. Under standard electrophoresis setups, negatively charged samples migrate toward the positively charged electrode (the anode). The hydrated gel network provides steric hindrance, so smaller molecules negotiate the pores more readily and run farther for a given time and voltage.
Step-by-Step Solution:
Verification / Alternative check:
Marker ladders (DNA size standards or protein prestained ladders) resolve into predictable bands whose migration is logarithmically related to size under constant buffer, gel concentration, and voltage—consistent with sieving plus constant charge-to-mass assumptions.
Why Other Options Are Wrong:
Common Pitfalls:
Confusing native PAGE (variable charge) with SDS–PAGE (normalized charge), or assuming DNA might migrate to the cathode; in typical TAE/TBE systems, DNA runs to the anode because it is negatively charged.
Final Answer:
All of the above
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