You have a protein. Its molecular weight is 144,000. If you treat the native pro

Question

You have a protein. Its molecular weight is 144,000. If you treat the native protein with either mercaptoethanol or urea, the molecular weight is unchanged. If you treat the native protein with both mercaptoethanol and urea, you get what appears to be a single type of component with a molecular weight of 18,000. After treatment with both reagents, only one band is detected on SDS gels or starch gel electrophoresis without SDS [large pores], and in the ultracentrifuge. (After treatment, the mercaptoethanol and/or urea are removed by dialysis, and the protein is kept in dilute solution)

A. The quaternary structure of the native protein is held together by (weak bonds) (covalent bonds) (both) (neither) (can't tell from info given).

Explanation / Answer

Both. Since it takes both urea and mercaptoethanol to separate the protein into subunits, both weak bonds and S-S bonds must connect the subunits.

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