Hello
I am currently working with a recombinant protein that has a tendency to aggregate and precipitate spontaneously during purification. According to the amino acid sequence it has a high alpha-helix content and a predicted coil-coil structure. It is not a membrane protein. Any suggestions what to add to the buffers to keep the protein soluble? I do not want to use potentially harmful substances eg SDS or trifluoroethanol, a stabilizer of the alpha-helical conformation. I appreciate any suggestions and references that could be of help to solve my problem.
Thanks in advance
Tomas Bratt
tob at ssi.dk
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