Denatured protein

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Maatomaat
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Denatured protein

Post by Maatomaat » Fri Nov 25, 2011 5:45 am

Is there any possible way to fix denatured protein?
The most difficult step is first step.
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JackBean
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Post by JackBean » Fri Nov 25, 2011 7:10 am

how is it denatured? You can try to dissolve it in urea and then decrease slowly concentration of urea, that should lead to folding.
http://www.biolib.cz/en/main/

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Maatomaat
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Re:

Post by Maatomaat » Fri Nov 25, 2011 7:48 am

JackBean wrote:how is it denatured? You can try to dissolve it in urea and then decrease slowly concentration of urea, that should lead to folding.


For example Acidic environment cause it.
urea what you said, is one of the denaturant factors. How and why can it be used at folding it?
The most difficult step is first step.
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JackBean
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Post by JackBean » Fri Nov 25, 2011 12:44 pm

that was just idea, since I know, that proteins are sometimes extracted with the use of urea and then refolded during dialysis. But with the acidic environment it should work as well. Slowly increasing pH and the protein could refold.
http://www.biolib.cz/en/main/

Cis or trans? That's what matters.

want2be
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Re: Denatured protein

Post by want2be » Sat Nov 26, 2011 3:23 am

i asked the same question to my bio teacher, and apparently there is no possibility that denatured protein can be fixed, unless someone have found something to fix the denatured protein

Cat
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Re: Denatured protein

Post by Cat » Sun Nov 27, 2011 5:47 pm

want2be wrote:i asked the same question to my bio teacher, and apparently there is no possibility that denatured protein can be fixed, unless someone have found something to fix the denatured protein


Incorrect.
It will depend on the protein. If it is capable of spontaneous folding, it will probably refold when environment returns to normal. If it needs chaperones to help it fold, it would not refold. Ex: water soluble proteins are more likely to refold than membrane proteins.

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