Question

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A new protein of an unknown structure has been purified. gel filtration revealed that the native protein had a molecular weight of 240,000 Da whereas SDS-PAGE electrophoreses shows two peaks of 80,000 da and 40,000 da. The results of the same experiments performed in presence of dithiothreitol are identical to results obtained in absence of DTT. explain what can be determine about the structure of this protein.

Answer 1

From the above experiment we can conclude that the protein has a quarternary structure, i.e. it is made up of multiple monomeric protein subunits.

Actual weight of the protein molecule is 2,40,000 Da. We conclude this from the above experiment using SDS-PAGE which shows two peaks at 80,000 Da and 40,000 Da which are individual monomeric subunits of the given protein.