Good evening,
My question is related to protein precipitation and analysis of its secondary structure; I have been facing this problem for the last 2 months. I have to do cd spectroscopy for the secondary structure of the protein, but before cd during dialysis, the protein is used to get precipitated. Then, I increased the ion concentration of Nacl from 300mM to 400mM. Now, it's not getting precipitating. However, the problem is that the higher concentration of ions affects the cd spectroscopy, gives a highly noisy signal, and the htv(high tension voltage) value is more than 700.
Would you like any suggestions on how I can overcome this problem? It would be a blessing to have any suggestions from you.
Thanks
Mohd Javed
Circular Dichroism (CD) is an excellent analytical techniques for rapidly determining of the secondary structure of proteins those have folding properties.
I am thinking, I can try to use salts having lower concentrations and also transparent buffer solution to maintaining the PH of the solution. It should be noted that buffer solution components have low absorption in the UV region.It would be clear if the spectra analysis deeply maintained.
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