I need help in knowing what atomic bonds/stretching/bending each peak occurred and how can it relate to the chemical structure of BSA? If you have a picture of the chemical structure of BSA, that would be highly appreciated.
I have attached 6 articles that the wave length range and the assigned groups have been presented in details.
For me your spectrum looks like that of pure water. You have to enrich your sample somehow.
I agree with Thomas Mayerhöfer - this is pretty much pure water.
I would suggest making a range of concentrations of pure BSA so you can visualise when the BSA features emerge from the background water.
In the attached, you can see an example for gelatine.
Use the time dependence of the frequency shift (Δf) of the resonator after adsorption instead of a solitary one. The time dependence of the mass (Δm) of the resonator after adsorption.
The lines must show the theoretical estimates for different conformations: 1. N form of BSA with side-on adsorption, 2. N form of BSA with flat-on adsorption, 3. E form of BSA with flat-on adsorption. The E form of BSA with side-on adsorption will be based on your test.
1.QCM data clearly indicate that structural changes of the albumin significantly affect the topography of layers formed on the surface.
2.Contact angle values are very sensitive to the structure of BSA monolayers formed on the silica surface.
3.Atomic Force Microscopy (AFM) method revealed various BSA structures depending on the pH at which they were adsorbed.
4.Conformational changes of BSA are reflected in both the measured values of the contact angle and the thickness of the protein layers measured using the QCM-D method.
For pH larger than 5.4 and smaller than 4.5 a monotonic decrease of the adsorbed mass is obvious. Using Atomic Force Microscopy (AFM) method would reveal various BSA structures depending on the pH at which they were adsorbed.
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