A new oscillator model with different form of the nonminimal substitution within the framework of the DuffinKemmer-Petiau equation is offered. The model possesses exact solutions and a discrete spectrum of high degeneracy. The distinctive property of the proposed model is the lack of the spin-orbit interaction, being typical for other relativistic models with the non-minimal substitution, and the different value of the zero-point energy in comparison with that for the Duffin-Kemmer-Petiau oscillator described in the literature.

We demonstrated the possibility of using LDF method to achieve predictive value in the detection of microcirculatory disorders in an individual patient with diabetes. This extends the perspectives of the method beyond the purely scientific research.

A new approach to the relativistic treatment of the fermion-boson system, based on the extension of the SL(2, C) groupTheoretical Physics Department Dniepropetrovsk National University 72 Gagarina av., Dniepropetrovsk 49050, Ukraine Abstract A new technique for constructing the relativistic wave equation for the two-body system composed of the spin-1/2 and spin-0 particles is proposed. The method is based on the extension of the SL(2, C) group to the Sp(4, C) one. The obtained equation includes the interaction potentials, having both the Lorentz-vector and Lorentz-tensor structure, exactly describes the relativistic kinematics and possesses the correct one-particle limits. The comparison with results of other approaches to this problem is discussed.

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Post-translational processing leads to conformational changes in protein structure that modulate molecular functions and change the signature of metabolic transformations and immune responses. Some post-translational modifications (PTMs), such as phosphorylation and acetylation, are strongly related to oncogenic processes and malignancy. This study investigated a PTM pattern in patients with gender-specific ovarian or breast cancer. Proteomic profiling and analysis of cancer-specific PTM patterns were performed using high-resolution UPLC-MS/MS. Structural analysis, topology, and stability of PTMs associated with sex-specific cancers were analyzed using molecular dynamics modeling. We identified highly specific PTMs, of which 12 modified peptides from eight distinct proteins derived from patients with ovarian cancer and 6 peptides of three proteins favored patients from the group with breast cancer. We found that all defined PTMs were localized in the compact and stable structural motifs exposed outside the solvent environment. PTMs increase the solvent-accessible surface area of the modified moiety and its active environment. The observed conformational fluctuations are still inadequate to activate the structural degradation and enhance protein elimination/clearance; however, it is sufficient for the significant modulation of protein activity.