Refolding denatured protein

IJ Huang gr8bn at cc.usu.edu
Tue Feb 27 20:04:20 EST 1996


In article <4grq5q$c53 at sci3.sri.ucl.ac.be> "P. Mertens" <mertens at toxi.ucl.ac.be> writes:
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>Subject: Re: Refolding denatured protein
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>From: "P. Mertens" <mertens at toxi.ucl.ac.be>
>Date: 26 Feb 1996 08:14:50 GMT
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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
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