Problem:
You are studying a new protein. The molecular weight of this protein as determined by gel filtration (size exclusion chromatography) is 350kD. When the protein is subjected to SDS-PAGE , there are 3 bands with molecular masses of 200, 125, and 25. When the protein is subjected to SDS-Page in the presence of 2-mercaptoethanol (2-ME), there are 3 bands with molecular masses of 100, 125, and 25.
Required:
Question 1: Please describe the tertiary structure of the full protein, including the number of subunits comprising the protein as well as subunit molecular weight. Also describe any interactions or forces that exist between the subunits.
Question 2: Draw the gel electrophoresis pattern for the SDS-PAGE experiment described in 1A. Be sure to include 3 lanes:
(1) a molecular weight marker lane indicating known molecular weights;
(2) a lane showing the protein in the absence of 2-ME, and
(3) a lane showing the protein in the presence of 2-ME.
Does anyone know how to go about this search to explain it.