My peptide has a siRNA binding domain. After synthesis and purification of peptide through Ni-NTA chromatography under denaturing conditions my protein would aggregate, so I added 10 mM arginine to prevent aggregation and checked the protein through SDS page. To check the activity of the protein, a gel shift assay was done which showed no change. the bands were of the same intensity. Is it possible that Arginine interefered with the siRNA binding to my protein and prevented it from binding? And what can I do to prevent my protein from getting aggregated during refolding.
Thanks in advance!
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