If you are going to determine the molecular weight of a protein with gel electrophoresis, why is it necessary to treat the protein with SDS? But if you want to isolate native proteins, like enzymes that still have activity within the gel, why would you not add SDS to the gel or fluids involved with the gel electrophoresis?

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∻Answer∻ ⚹ To determine the molecular weight of a protein with gel electrophoresis, it is necessary to treat the protein with SDS. However, if you want to isolate native proteins, like enzymes that still have activity within the gel, you would not add SDS to the gel or fluids involved with the gel electrophoresis. ⚹ ∻Solution∻ ‖ a ⋮ SDS (Sodium Dodecyl Sulfate) is an anionic detergent that denatures proteins by binding to the polypeptide chains and imparting a negative charge. This allows the proteins to be separated based on their molecular weight during gel electrophoresis. ‖‖ b ⋮ When isolating native proteins, such as enzymes, it is crucial to maintain their functional conformation. Adding SDS would denature these proteins, rendering them inactive. Therefore, SDS is not used in this context to preserve the native structure and activity of the proteins. ‖ ∻Key Concept∻ ⚹ SDS denatures proteins and imparts a negative charge for molecular weight determination. ⚹ ∻Explanation∻ ⚹ SDS is used in gel electrophoresis to denature proteins and separate them based on molecular weight. However, for isolating native proteins, SDS is avoided to maintain their functional conformation and activity. ⚹◊How does the addition of SDS affect the migration of proteins in gel electrophoresis⍭ Generate me a similar question◊

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