simon sham wrote:
Hi,
I have a question of using Radius of Gyration to analyze my simulation
data for a protein at a temperature that it would unfold.
My understanding is that when a protein in an unfolded state, it still
have some structure and is not a random coil. So, my question is:
Will the Rg value for a unfolded protein be completely different from
that of folded one?
In general, probably. It depends entirely upon what the "unfolded" state is for
the protein in question - is it elongated, with little secondary structure, or
does it collapse into a disordered globule that doesn't resemble the native
state? If the latter, then Rg can be misleading. At extremely high
temperature, though, I would expect just about any protein to be very elongated,
unless it has lots of disulfides to keep it compact.
-Justin
--
========================================
Justin A. Lemkul
Ph.D. Candidate
ICTAS Doctoral Scholar
MILES-IGERT Trainee
Department of Biochemistry
Virginia Tech
Blacksburg, VA
jalemkul[at]vt.edu | (540) 231-9080
http://www.bevanlab.biochem.vt.edu/Pages/Personal/justin
========================================
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