Refolding denatured protein

IJ Huang gr8bn at
Tue Feb 27 20:04:20 EST 1996

In article <4grq5q$c53 at> "P. Mertens" <mertens at> writes:
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>Subject: Re: Refolding denatured protein
>Message-ID: <4grq5q$c53 at>
>From: "P. Mertens" <mertens at>
>Date: 26 Feb 1996 08:14:50 GMT
>References: <4girf2$dnp at>
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>An important thing is to keep the concentration of refolding protein 
>sufficiently low to prevent aggregation caused by interaction 
>of hydrophobic parts of the protein that are transiently exposed during 
>the renaturation. Especially in the case of renaturation by dialysis, all 
>the molecules are in the same renaturing state at each moment of the 
>dialysis, so that the concentration of exposed hydrophobic groups becomes 
>quite important at a certain time during the process. You should perform 
>your dialysis on dilute protein preps and concentrate afterwards.

Include reducing agents such as DTT and reduced glutathione will also help 
the refolding process.

Ijen Huang
Graduate Student
EMAIL:GR8BN at CC.USU.EDU               ll          Dept. of Biology
HTTP://CC.USU.EDU/~GR8BN/HUANG.HTML  ll        Utah State University
PHONE: 1-808-797-2724                ll       Logan, Utah 84322-5305
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