00:01
Okay, so we have a protein with a molecular mass of 400 kilodotans, but measured by a sized exclusion chromatography.
00:08
And then when subjected to gel electrophoresis, in the presence of sds, the protein gives, shown here in blue, a 180 kilodotton fragment, on 160 kiladulton fragment, and a 60 kiladulton fragment, which adds up to 400 kilatulthens.
00:24
When electrophyses carried out in the presence of sds and dithio -3 -tol, otherwise known as dtt, the three bands are again formed, but this time it's 160, 90, and 60 -kalladaltans.
00:39
Determine the subunit composition of the protein and clearly explain how you came to this determination.
00:46
So the thing with dtt is that this, this reduces disulfide bonds.
01:03
So it is used in terms of proteins, and especially in this context, protein gel, electrolysis, it's used to further denature the protein.
01:21
Why would we further denature the protein for better size? separation...