Nucleoid-Associated Proteins HU and IHF: Oligomerization in Solution and Hydrodynamic Properties.

Structure and function of bacterial nucleoid is controlled by the nucleoid-associated proteins (NAP). In any phase of growth, various NAPs, acting sequentially, condense nucleoid and facilitate formation of its transcriptionally active structure. However, in the late stationary phase, only one of the NAPs, Dps protein, is strongly expressed, and DNA-protein crystals are formed that transform nucleoid into a static, transcriptionally inactive structure, effectively protected from the external influences.

Structural Insights into Iron Ions Accumulation in Dps Nanocage.

Dps (DNA-binding protein from starved cells) is well known for the structural protection of bacterial DNA by the formation of highly ordered intracellular assemblies under stress conditions. Moreover, this ferritin-like protein can perform fast oxidation of ferrous ions and subsequently accumulate clusters of ferric ions in its nanocages, thus providing the bacterium with physical and chemical protection. Here, cryo-electron microscopy was used to study the accumulation of iron ions in the nanocage of a Dps protein from .

Model of Decision Making Support for a Doctor in the Treatment of an Oncosurgical Patient in a Hospital.

At the present moment, there is no uniform approach to the decision to conduct a planned surgical intervention in case of oncosurgical pathology, with appropriate recommendations in different sources. Consequently, in modern medicine, there is a particular problem of an objective assessment of the patient's physical condition and a risk assessment of an upcoming surgical intervention for developing an individualized tactic of preparation for surgical treatment for each particular patient. The need for introduction of new approaches and technologies, as well as treatment regimens, that allow us to take a fresh look at the possibilities of solving the problems of predicting critical outcomes of planned operations, determined the purpose of our study.