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Effect on protein of low pH?

buffer protein degradation pH

Best Answer mdfenko, 21 April 2016 - 05:27 AM

there is a slight possibility of acid hydrolysis of peptide bonds.

 

neutralization may return the protein to its native conformation. but, extended exposure to low pH may irreversibly denature the protein. it's always best to adjust the pH as soon as possible.

 

when collecting protein eluted with low pH, we add a cushion of buffer to the collection tube so that the pH will adjust as it's collected.

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#1 Michael Starr

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Neutral

Posted 20 April 2016 - 01:06 PM

Say I leave a protein in pH 2.7 for a day. Will anything happen to it besides denaturation? It won't cleave or anything, will it? And if I re-neutralize it after that, will it reach its native conformation once again?



#2 mdfenko

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Posted 21 April 2016 - 05:27 AM   Best Answer

there is a slight possibility of acid hydrolysis of peptide bonds.

 

neutralization may return the protein to its native conformation. but, extended exposure to low pH may irreversibly denature the protein. it's always best to adjust the pH as soon as possible.

 

when collecting protein eluted with low pH, we add a cushion of buffer to the collection tube so that the pH will adjust as it's collected.


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