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Protein separation methods

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Protein separation methods

Postby pinkypig on Thu Apr 17, 2008 10:56 pm

Hi i want to know which of the below mentioned methods are best for :
(a) simply to remove protein from the solution,
(b) wanting to recover the precipitated protein in its normally folded state?


•Disruption of the hydrogen bonds, which hold the molecule in its three-dimensional conformation
•Removal of the water of hydration of the protein
•Generation of a net positive charge on the surface of the protein and the formation of an insoluble complex with an anion
•Formation of an insoluble complex with heavy metals
•Adsorption onto a precipitate caused by a chemical reaction between protein precipitating agents
•Unfolding of the polypeptide chain by strong oxidising acids which cause all of the surface of the protein to be positively charged and the subsequent repulsion between these like charges
•Alteration of the nature of the solvent such that the presence of hydrophobic groups in the centre of the protein is no longer the most favourable orientation
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Postby mith on Fri Apr 18, 2008 1:33 am

Wouldn't (a) depend on what it's mixed with i.e. what it needs to be separated from?
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Postby pinkypig on Fri Apr 18, 2008 1:51 am

no
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