Rather than looking at "anti-DTT" it is more important to set up an
appropriate redox system. This can be a combination of reduced and
oxidised glutathione  or cysteine. If you check some of the commercial
protein refolding screens this should give you an idea about relative
concentrations.

 

Best regards,

Paul..

 

------------------------------------------------------------------------
-----------------

Dr. Paul A. McEwan

Senior Scientist (Structural Biology)

Evotec (UK) Ltd.

114 Innovation Drive | Milton Park | Abingdon | Oxfordshire | OX14 4SA

 

email: paul.mce...@evotec.com <mailto:paul.mce...@evotec.com> 

Tel: +44 (0)1235 861561

Fax:+44 (0)1235 863139

direct line: +44 (0)1235 838802

www.evotec.com <http://www.evotec.com> 

 

From: CCP4 bulletin board [mailto:CCP4BB@JISCMAIL.AC.UK] On Behalf Of
Jacob Keller
Sent: 28 February 2013 11:09
To: CCP4BB@JISCMAIL.AC.UK
Subject: Re: [ccp4bb] disulfide engineering

 

Along these lines, what reagents do people use to promote disuflide
bonds, i.e., the "anti-DTT?"

 

JPK

On Thu, Feb 28, 2013 at 2:06 AM, David Briggs <drdavidcbri...@gmail.com>
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" <careinaedgo...@yahoo.com>
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: j-kell...@northwestern.edu
******************************************* 


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