Interface Ba2
In order to study the possible binding of the HSV-1 receptor, the interaction of Omicron BA.2 RBD with the membrane-anchored hACE2 was modeled by using cryo-EM structure of the Omicron BA.2 RBD-hACE2. This structure is shown in Figure 2a. The model of the interface was based on the crystal structure of the glycoprotein D of HSV-1 and the cryo-EM structure of the trimeric spike complex of the virus, published recently (Lok et al. 2014). The comparison of the two models shows that no significant differences exist between both structures. This result indicates that the main part of the RBD forms a stable three-helix bundle, which is very similar to that of the WT RBD. The main difference is that the Omicron BA.2 RBD has an extra helix between helix 2 and helix 3. This helix is not involved in the interaction with the receptor hACE2, and the two proteins only contact each other in two small domains (Figure 2b ). We speculated that this helix is located inside the virus envelope, outside of the cell, and it is not able to affect the virion binding to the cell receptor, but it is only a conformationally sensitive region that possibly affects the stability and the antigenicity of the virus. The residues in the interface of both proteins are involved in the interactions with each other, and they are different from those of WT RBD. This might be due to the substitution of Ba2+ ions for Ca2+ ions during the crystal structure preparation. In the Omicron BA.2 RBD the number of the salt bridges is almost twice higher in comparison with WT RBD. The possible reason is that substitution of Ba2+ ions for Ca2+ ions may result in the flexibility of the regions neighboring the interface, which could cause the stabilization of the conformation of the viral proteins, and the substitution of Ba2+ ions for Ca2+ ions may also lead to the increase of the number of the salt bridges. At the interface in the WT RBD structure, there is one hydrogen bond (H bond) formed between residues N255 and D345 in a similar way as in the Omicron BA.2 RBD-hACE2 complex. The thermal stability analysis carried out to probe this possible H bond may clarify this hypothesis (Figure 2d ). It is known that substitution of Ba2+ ions for Ca2+ ions may result in the weakening of the H bond between the key residues of N255 and D345. In the case of the virus, this could influence the conformation of the RBD, and it could affect the stability and antigenicity of the virus. It should be noted that the substitution of Ba2+ ions for Ca2+ ions, which induced the conformational flexibility of the RBD, also induced a conformation flexibility of the hACE2. It is necessary to note that in the case of the WT RBD-hACE2 complex, a H bond forms between residues N255 and D345 (Lok et al. 2014), which can stabilize the receptor hACE2; however, in the Omicron BA.2 RBD-hACE2 complex, substitution of Ba2+ ions for Ca2+ ions weakened this H bond, which did not stabilize the receptor.
compositional profiles and oxygen profiles of a ybacuo system in a melt-textured layer of a resistive cuprate high-temperature superconductor, grown by co-evaporation of metallic constituents on mgo(100) in (9-anthanthiadecanate)(ch3cs2). higher o contents in the ba-rich region was revealed.
the co-existence of two different phases in the highly resistive c-axis oriented ybacuo superconductor, sample ybco-2, grown by metallic oxide reactive co-evaporation on mgo(100) was examined. the superconducting transition of a c-axis oriented, non-reactive ybacuo thin film (sample ybco-1) grown in the same way on a sapphire substrate was also measured.
x-ray diffraction and transmission electron microscopy were used to examine the c-axis oriented ybacuo films grown by co-evaporation of metallic constituents on mgo(100) in (9-anthanthiadecanate)(ch3cs2). compositional analysis and structural information were obtained.
the authors have developed a new technique for the preparation of high-quality ba- and sr-doped ba2sio4 single-crystal films by the reactive co-evaporation of metallic constituents (ba, sr) on mgo(100). the growth mechanism of the ba- and sr-doped ba2sio4 films is discussed. the compositional, structural and dielectric properties of the ba- and sr-doped ba2sio4 films with different doping contents were examined using x-ray diffraction, atomic force microscopy, electron energy-loss spectroscopy, and dielectric measurements.
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