Dear Tom, I think you have to do fluorescence suppression measures and fluorescence lifetime measurements to determine the constant interaction between the polymer and the protein. Thus, the addition of the polymer solution in the protein solution may change the pH of the solution. So, I suggest you initially make studies of the effect of pH and DMF in your protein. Since then, perform the suppression study of protein fluorescence in buffer solution have the same pH of the DMF. If possible, adjust the pH of the DMF ph that promotes maximum quantum efficiency of protein fluorescence.

Hi Navin, proteins don't do well in DMF. I suggest that you make a highly concentrated solution of your polymer in DMF, dilute it in buffer and use the same dilution of DMF as your control.

Thank you Dr. Stefansson and Dr. Ferreira, My polymer will ppt out if I add water or the buffer and I wont be able to complete my studies. Can I do the fluorescence studies of proteins in DMF first and use it as baseline for studies with polymer in DMF in same amount. So i will get NET fluorescence data?

Hi Navin, 100% DMF will probably denature your protein.

Have you tried doing serial dilutions of your DMF solubilized polymer into buffer to see when it precipitates? Also you could try doing serial dilutions into buffer containing 10% glycerol, which is well tolerated by most proteins.