I want to determine the binding affinity of my protein-metal ion complex using anisotropy. The protein has been FITC-labelled. I am using 500nM protein concentration. The anisotropy value decreases as I increase the metal ion concentration and then reaches saturation.
The metal-bound protein of interest has a compact shape and a significantly smaller size as compared to the unbound protein.
As I know anisotropy is affected by the rate of rotational diffusion of the molecule which depends upon apparent molecular size. Small-sized molecules tend to rotate rapidly and depolarize light as compared to larger ones.
So, my question is can the binding of the metal ion to my protein (which causes compaction and size reduction) be the reason for the decreasing anisotropy value with increasing metal ion concentration?
Thanks in advance.
Tushar Chakraborty
Your protein, together with the metal ion in the water, is a watery quantum material. We discovered this kind of quantum materials. New quantum materials are aqueous solutions of ionic surfactants and polyelectrolytes in the area of extended phase transitions. In your case, the transition (protein folding) occurs under the action of the added metal ion. In this case, the anisotropy coefficient changes due to the quantum chaos of water and protein. When the anisotropy coefficient reaches a plateau, it is no longer a quantum material. We have submitted an application for an invention for polyelectrolytes and we are awaiting a decision on this issue. You can read more about new quantum materials in our articles and patents.
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