## 3 Results and Discussion
### Study of the Physicochemical Properties of Aqueous IgG Colloid of Different Concentrations
Thus, it has been shown that when stirring in a turbulent flow, variations in the physicochemical properties of H\({}_{2}\)O and aqueous colloids of the IgG protein are observed. Exposing the solutions described above to magnetic fields has no effect on water. However, in protein solutions, some parameters change. It is interesting to note that protein solutions are more susceptible to the action of alternating magnetic fields with a frequency of 8 Hz, and less subject to magnetic fields with a frequency of 50 Hz. After exposure to a magnetic field or mechanical stirring, measurements were taken as quickly as possible. It should be taken into account that moving the test tubes from the exposure installation to the measurement installation several meters away, pouring liquid into optical cuvettes, and moving the optical cuvette into the device takes some time (about half a minute). The measurement itself also has a duration from several seconds to several tens of seconds. It is known that the physical properties of water after the cessation of physical impact often return to control values quite quickly (from fractions of seconds to tens of seconds) [80; 81; 82]. In this case, changes in the secondary structure of protein molecules occur orders of magnitude slower due to steric restrictions. For example, after exposure to ionizing radiation, relaxation of long-lived radical forms of proteins occurs within several days [83]. In this work, the parameters of colloidal protein solutions were measured (not pure water and not dry protein molecules). In order to find out how long changes in the physicochemical properties of aqueous IgG colloids persist after exposure to a magnetic field and mechanical action, several series of experiments were carried out (Figure 8). Figure 7: Change in the refractive index (**a**) and fluorescence intensity (**b**) of aqueous colloid of IgG protein molecules after exposure to alternating magnetic field with frequencies of 8 and 50 Hz, as well as mechanical stirring with frequencies of 4.4 and 12 Hz (M \(\pm\) SD, n = 6). The excitation wavelength when measuring fluorescence is 291 nm, and the protein concentration is 1 mg/mL. *—statistically significant difference relative to unexposed samples (_t_-test, \(p\) < 0.05). The duration of changes in the fluorescence intensity of aqueous IgG colloids after exposure to a magnetic field (8 Hz) and mechanical action (12 Hz) was studied (Figure 8a). It was shown that immediately after exposure to a physical factor, maximum changes in the fluorescence intensity of IgG colloids were observed. When exposed to mechanical shaking, the fluorescence intensity increased by approximately 5%; when exposed to a magnetic field, the fluorescence intensity decreased by a similar amount. In general, the data obtained are consistent with the data presented in Figure 7b. When exposed to mechanical shaking, the increased fluorescence intensity compared to the control persisted for at least 10 min. When exposed to a magnetic field for at least 5 min, the luminescence intensity remained reduced compared to the control. A total of 20 min after exposure, the fluorescence intensity did not differ from control values. The duration of change in the refractive index of aqueous IgG colloids after exposure to a magnetic field (8 Hz) and mechanical influence (12 Hz) was studied (Figure 8b). It has been shown that when exposed to a magnetic field for 20 min, no significant change in the refractive index of protein solutions is observed. When exposed to mechanical shaking, the refractive index increased by approximately 3 \(\times\) 10\({}^{-6}\), which is consistent with the data presented in Figure 7a. The difference in the refractive index in the group subjected to mechanical action relative to the control is observed for at least 5 min. The duration of change in the optical density of aqueous IgG colloids after exposure to a magnetic field (8 Hz) and mechanical action (12 Hz) was studied (Figure 8c).