I am trying to find at least 1 good article that describes clearly the molecular mechanism behind protein precipitation with PEG6000.
For some reason I'm not able to find thin information clearly decribed
Polyethylene glycol precipitates proteins by excluding water from the protein surface but not the interior of the protein. The protein crashes out of solution with exclusion of water. If the right cocktail of conditions of pH buffer type salt and salt concenration and PEG type 1000, 3350, 4000, 6000 etc. and PEG concentration exist the protein will crash out as a crystal rather than an amorpous precipitate.
Polyethylene glycols have been more successful in protein crystallization than high ionic strength using salts to salt-out a protein from solution. If you are just trying to precipitate a protein for some kind of purification procedure, I would recommend you use ammonium sulfate instead.
Adron Ung In your opinion, which method for protein precipitation is the best? As, i do acetone precipitation but at the end i mostly get very low concentrations.
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