[RASMB] smaller protein size than expected

[Arthur Rowe]

Fang

Which optics were you using - absorption or interference? If the latter,
then you may have problems with the 'baseline' if that has been floated.

Whatever, a sigma value of the order of >1 ought to be fine to get a value
seriously better than '10kDa for a 16kDa protein"

Arthur


hello all,

I recently did sedimentation equilibrium runs on a protein (monomer size: 16
KD), at 3 concentrations (260, 130, 52 u M) at speeds of 25, 30, 35000 RPM.
Using Heteroanalysis, I could only fit the data into an ideal solution
model,
with a monomer MW of 10KD.  Also, this protein runs at a MW lower than
expected
on the gel filtration col also. SDS gel indicates it's the right size and
not
degraded after the measurements.

Anybody has any suggestions why this protein appears to be such a "smaller"
protein?

Thanks a lot,

Fang Yi
Postdoc Fellow
Yale University
Molecular Biophysics and Biochemistry
New haven, CT 06511
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