Dear Professor Ethan,
I apologize, for the partial
information provided by me in the second email. For the *in vivo* assembled
(as-purified) protein, we have confirmed the [4Fe-4S] cluster by CD and
EPR. From the 415/280 ratio and Ferrozine assay, we have
On Monday, March 19, 2018 2:20:50 PM PDT PULSARSTRIAN wrote:
> Dear Professor Diana,
>
> Thank you very much for your
> comment, and we will certainly look at, if ‘domain swapping’ is any reason
> for the trimeric nature of the protein.
>
>
Dear Professor Diana,
Thank you very much for your
comment, and we will certainly look at, if ‘domain swapping’ is any reason
for the trimeric nature of the protein.
There are two cysteines in helix-1 and two cysteines
in helix 3.
Is it possible that you have a case of domain swapping that causes the trimeric
assembly?
Diana
**
Diana R. Tomchick
Professor
Departments of Biophysics and Biochemistry
University of Texas Southwestern Medical Center
5323 Harry Hines Blvd.
Rm.
Dear all,
Sorry for the slightly off-topic question.
I am working on a non-native, *de novo* [4Fe-4S]
protein, designed as a four-helix bundle. The *in vitro* reconstituted
protein assembles with [4Fe-4S] (confirmed by EPR) and exists in
monomer-dimer
