1. Why doesn\'t native gel electrophoresis usually separate proteins effectively

Question

1. Why doesn't native gel electrophoresis usually separate proteins effectively by molecular weight? What else contributes to the separation? How does the use of sodium dodecyl sulfate in denaturing PAGE overcome the size-dependence problem with native gel electrophoresis? What type of proteins should work? What is their common property? 2. Why do we use the SDS-PAGE technique in Week 4? What is our purpose in terms of 3. Why do we include protein standards (marker proteins) when running the gel sample characterization?

Explanation / Answer

3.Ans-
    The standard proteins are a tertiary or quaternary structure of a protein that suitable for native SDS-PAGEs. They can determine the KDa of a band(s) that formed when gel running. Therefore, suitable protein marker is used to estimate the size of proteins.

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