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Which of the following techniques could help improve the purity of a protein sample while maintaining the protein's native state?
The only choice that would actually be useful in improving the purity of a protein sample would be column chromatography. It is possible to attach a specific ligand to your protein of interest to help separate it from a mixture via this method.
SDS-PAGE results in a separated, but denatured, protein sample. Detergents used in this process damage the protein structure, making it impossible to retain the native state. Southern blotting is a technique used to identify specific sequences of DNA in a sample and has nothing to do with increasing the purity of a protein sample.
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