In this work, based on the method of infrared emission spectroscopy, the study of emission spectra of interferon-gamma (IFNγ) solution in a mixture or surrounded by three low-concentration solutions (IFNγ, antibodies to IFNγ, glycine buffer) or water control was performed. First of all, the solutions of low concentrations themselves were studied. It was shown that low-concentration solutions of IFNγ and antibodies to IFNγ had lower emission intensity in three spectral bands near 800, 1,300 and 2000 cm−1 compared to water control. Glycine buffer solution had a radiation level indistinguishable from that of the control. In this work, the effect of adding these low-concentration solutions to IFNγ (1 mg/ml) was compared to the effect of adding water control to IFNγ. All solutions or water were added in 10% (v/v). It was found that adding each of the three test solutions induced an increase in the radiation intensity of the IFNγ solution in the spectral range of 400–1700 cm−1 (compared to the IFNγ solution with control spike). It was also tested whether the radiation of the studied low-concentration solutions surrounding the IFNγ solution (1 mg/ml) affected the IFNγ radiation. The measurement results were compared to the data obtained for IFNγ surrounded by water control. All three solutions were found to exert a distant effect on the IFNγ solution (1 mg/ml), which was manifested in a decrease in the intensity of its radiation near 1,000 and 1,500 cm−1 compared to the control solution of IFNγ. Thus, the emission spectra of low-concentration aqueous solutions were measured for the first time, and differences in the emission spectra of the IFNγ solution depending on low-concentration additives and the environment were shown. The paper interprets the observed differences and discusses possible mechanisms underlying the observed phenomena.

ATP is one of the main biological molecules. Many of its biological and physicochemical properties, such as energy capacity of the phosphate bonds, significantly depend on hydration. However, the structure of the hydration shell of the ATP molecule is still a matter of discussion. In this work, the hydration shells of ATP in water and MgCl 2 solutions were examined by terahertz time-domain spectroscopy and dynamic light scattering. Terahertz spectroscopy reveals the distorted water structure in the ATP water solution displaying tightly bound water molecules, which could be explained by the hydration of phosphate groups. Upon ATP binding to a Mg 2+ ion, the situation is principally different: Instead of the distorted water structure, its arranged structure with increased hydrogen bond number is observed. Dynamic light scattering showed that the hydrodynamic diameter of ATP increases by 0.5 nm after Mg 2+ binding. Meanwhile, according the characteristics of scattering, the increase of the shell size occurs via formation of a layer with a refraction coefficient similar to water. This layer can be interpreted as hydration shell differing from unaltered water by increased number of hydrogen bonds.

Hydration plays a fundamental role in DNA structure and functioning. However, the hydration shell has been studied only up to the scale of 10–20 water molecules per nucleotide. In the current work, hydration shells of DNA were studied in a solution by terahertz time-domain spectroscopy. The THz spectra of three DNA solutions (in water, 40mm MgCl2 and 150 mM KCl) were transformed using an effective medium model to obtain dielectric permittivities of the water phase of solutions. Then, the parameters of two relaxation bands related to bound and free water molecules, as well as to intermolecular oscillations, were calculated. The hydration shells of DNA differ from undisturbed water by the presence of strongly bound water molecules, a higher number of free molecules and an increased number of hydrogen bonds. The presence of 40 mM MgCl2 in the solution almost does not alter the hydration shell parameters. At the same time, 150 mM KCl significantly attenuates all the found effects of hydration. Different effects of salts on hydration cannot be explained by the difference in ionic strength of solutions, they should be attributed to the specific action of Mg2+ and K+ ions. The obtained results significantly expand the existing knowledge about DNA hydration and demonstrate a high potential for using the THz time-domain spectroscopy method.

Ultrastructure of the neuropil of the brain oculomotor nuclei was studied in mice after 30-day exposure to microgravity on Bion-M1 biosatellite and after 13-h exposure to Earth gravity. The number of axo-dendritic synapses in the neuropil of the oculomotor nucleus significantly decreased after the flight. Degenerated axon terminals containing conglomerates of presynaptic vesicles appeared. The number of synapses with high functional activity increased and the length of active zones of the axo-dendritic synapses significantly increased. The observed ultrastructural changes of the neuropil of the oculomotor nuclei of mice exposed to microgravity reflect the development of long-term deafferentation of the analyzed brain structures. These changes in the neuropil ultrastructure can determine the disturbances in the oculomotor system, e.g. development of atypical nystagmus under conditions of microgravity.

This paper describes a new method for measuring the spectra of infrared radiation emitted by protein solutions in the native state without any external excitation. Radiation is detected using a vacuum Fourier-transform infrared spectrometer, and the tested sample itself is a source of radiation. The necessary conditions for detecting radiation from a sample are the use of a highly sensitive cooled detector and the presence of a cold background. In this work, the background was a black body at the boiling point of nitrogen. It is also important to select the optimal vacuum pumping depth for the spectrometer and sample thickness. Radiation occurs due to spontaneous radiative transitions from excited vibrational energy states to the ground state of molecules. The intensity of radiation is determined by the population of the respective energy states, which, according to the Boltzmann distribution, depends on temperature and frequency. Using solution of human interferon gamma as an example, it has been shown for the first time that proteins have intrinsic radiation. The described method allows detecting spectral lines with a radiation power of about 10−8 W or even less. It has also been demonstrated that emission spectroscopy offers advantages in the signal-to-noize ratio compared to absorption spectroscopy and allows analyzing the structural characteristics of a protein, in particular, providing information about its secondary structure. Another significant advantage of the method described in the article is its noninvasiveness. At the sample temperature of 25°С, emission spectra can be detected in the range from 400 to 3,600 cm−1, which covers almost the entire frequency range of existing stretching and bending vibrations of molecules. At the same time, in the fingerprint region from 500 to 1,600 cm−1 (the most informative part of the infrared spectrum), the highest sensitivity of the method is demonstrated. There is also potential for extending the available frequency range into the far infrared and terahertz ranges. Being applicable to the study of protein solutions in low concentrations, the proposed approach is not only interesting from the point of view of fundamental science but also can have applied significance in biological and medical research.