In the literature, you can find examples of air oxidation, oxidized
glutathione (alone), mixture of reduced and oxidized glutathione, and
hydrogen peroxide. The correct concentrations have to be found
empirically. We are just now mushing through this with an engineered
disulfide variant. Air oxidation partially worked for us--one of the
engineered disulfides worked, one did not.
_______________________________________
Roger S. Rowlett
Gordon & Dorothy Kline Professor
Department of Chemistry
Colgate University
13 Oak Drive
Hamilton, NY 13346
tel: (315)-228-7245
ofc: (315)-228-7395
fax: (315)-228-7935
email: [email protected]
On 2/28/2013 7:55 AM, Clemens Grimm wrote:
Along these lines, what reagents do people use to promote disuflide
bonds,
i.e., the "anti-DTT?"
Glutathione (red) + Glutathione (ox), redox potential is adjusted by
varying the ratio.
Best,
Clemens
JPK
On Thu, Feb 28, 2013 at 2:06 AM, David Briggs
<[email protected]>wrote:
You might want to try "Disulfide by design"
http://cptweb.cpt.wayne.edu/DbD2/
Cheers
Dave
On Feb 28, 2013 6:55 AM, "Careina Edgooms" <[email protected]>
wrote:
Dear CCP4 members
I wish to engineer a disulfide bond at the dimer interface of a
protein I
am working with. Does anyone know of any available software to
assist with
this?
Best
Careina
--
*******************************************
Jacob Pearson Keller, PhD
Postdoctoral Associate
HHMI Janelia Farms Research Campus
email: [email protected]
*******************************************
--------------------------------------------------
Dr. Clemens Grimm
Institut für Biochemie
Biozentrum der Universität Würzburg
Am Hubland
D-97074 Würzburg
Germany
e-mail: [email protected]
phone : +49 0931 31 84031
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