Using imidazole and glycerol in the protein purification process can increase protein stability and solubility. What is the chemical mechanism for that?
This paper makes some good arguments:
http://www.ncbi.nlm.nih.gov/pubmed/19817484
A mentor was a bit less detailed when he said to me, many years ago, that glycerol "increases the aquicity of water"
Imidazole has no such general properties that I am aware of, but glycerol is often used in IMAC which sees high levels of imidazole.
Hi Paulo, just to expand on Edward's post, most proteins in vivo are not found in buffered aqueous media. They are surrounded with proteins, lipids and other organic molecules.
This environment keeps them stable. Through trial and error, biochemists have found that certain compounds, like glycerol, keeps proteins stable by mimicking their natural environment, which in many cases is a mixture of hydrogen and hydrophobic bonds.
Hi Paulo,
As Steingrimur said glycerol stabilize proteins and the specific molecular way it does is not completely clear. Some publication about this topic:
Vagenende, V., Yap, M. G. S., & Trout, B. L. (2009). Mechanisms of protein stabilization and prevention of protein aggregation by glycerol. Biochemistry, 48(46), 11084–11096. http://doi.org/10.1021/bi900649t
What brand and purity of glycerol do you use in protein purification/dialysis?
Thanks.
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