Which of the following purification techniques requires no modification of the protein?

Question

BlackTom AI · Accepted Answer

In evaluating purification approaches, we must determine which methods can separate or purify a protein without altering its sequence or adding tags.
Option a: Affinity purification typically relies on a specific interaction between the target protein and a ligand or tag (such as a His-tag with nickel or a FLAG tag). To create this interaction, the protein is often modified with a tag or the ligand is engineered, so this method generally requires modification of the protein or its environment. Therefore this choice is not correct for the question's constraint.
Option b: Size exclusion chromatography (also called gel filtration) separates proteins based on their hydrodynamic radius, not their sequence or chemical properties, and it does not require any modification of the protein. It preserves the native protein and function, making it a correct choice under the no-modification criterion.
Option c: Ion exchange chromatography separates proteins by charge differences on their surfaces and usually does not require any modification of the protein itself. The method leverages the protein’s intrinsic charge properties, so this is another correct choice for the question.
Option d: Mass spectrometry is an analytical technique used to determine mass-to-charge ratios and is not a purification method. While preparative purification can precede MS, MS itself does not purify the protein in the same way as chromatographic methods, and it often involves conditions or fragmentation that are not considered purification per se. Hence this option is not appropriate for the stated requirement.
Thus, the options that meet the criterion of requiring no modification are b. Size exclusion and c. Ion exchange.

BPS3021 S1 2025 CYL | Protein purification & characterisation

Which of the following purification techniques requires no modification of the protein?

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