How can we shift a protein's isoelectric point towards alkaline pH range maintaining cationic charge? What are the modification methods to achieve this without compromising proteins solubility?
The proteins isoelectric point is defined by amino acid sequence and you have to modify the protein itself to change the isoelectric point. See the recent article about milk proteins: http://www.biology-direct.com/content/6/1/40
You can predict the effect of change using Protein calculator, (for example: http://www.scripps.edu/~cdputnam/protcalc.html) if you know the primary structure of your protein. Insertion of Lys, Arg, His may result the desired shift.
One can use L-Arginine to maintain the cationic charge. However,Arginine is also effective in suppressing aggregation of proteins and may be beneficial to be included during purification processes. 20mM Arginine in protein buffer should be fine to maintain the cationic charges/ solubility index of the protein.
The proteins isoelectric point is defined by amino acid sequence and you have to modify the protein itself to change the isoelectric point. See the recent article about milk proteins: http://www.biology-direct.com/content/6/1/40
You can predict the effect of change using Protein calculator, (for example: http://www.scripps.edu/~cdputnam/protcalc.html) if you know the primary structure of your protein. Insertion of Lys, Arg, His may result the desired shift.
One of the paper. You can surely find many in relevance to it.
A simple method for improving protein solubility and long-term stability.
http://www.ncbi.nlm.nih.gov/pubmed/15264823
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