On the near horizon rotating black hole geometries with NUT charges

The near horizon geometries are usually constructed by implementing a specific limit to a given extreme black hole configuration. Their salient feature is that the isometry group includes the conformal subgroup SO(2,1). In this work, we turn the logic around and use the conformal invariants for constructing Ricci-flat metrics in d=4 and d=5 where the vacuum Einstein equations reduce to a coupled set of ordinary differential equations. In four dimensions the analysis can be carried out in full generality and the resulting metric describes the d=4 near horizon Kerr-NUT black hole. In five dimensions we choose a specific ansatz whose structure is similar to the d=5 near horizon Myers-Perry black hole. A Ricci-flat metric involving five arbitrary parameters is constructed. A particular member of this family, which is characterized by three parameters, seems to be a natural candidate to describe the d=5 near horizon Myers-Perry black hole with a NUT charge.Comment: 12 page

The Essence of the Digitalization Process as a New Global Informatization Stage

The article describes the essence of the term "digitalization" and shows the nature of this process. The impact on people's lives and globalization itself have been determined as a result of the conducted study. Particular attention has been drawn to digital transformation, its use in the business context and its impact on such organizations as government, government agencies and other institutions involved in addressing social and global issues such as pollution and aging, using one or more existing and new technologie

Effects of NMR spectral resolution on protein structure calculation

Adequate digital resolution and signal sensitivity are two critical factors for protein structure determinations by solution NMR spectroscopy. The prime objective for obtaining high digital resolution is to resolve peak overlap, especially in NOESY spectra with thousands of signals where the signal analysis needs to be performed on a large scale. Achieving maximum digital resolution is usually limited by the practically available measurement time. We developed a method utilizing non-uniform sampling for balancing digital resolution and signal sensitivity, and performed a large-scale analysis of the effect of the digital resolution on the accuracy of the resulting protein structures. Structure calculations were performed as a function of digital resolution for about 400 proteins with molecular sizes ranging between 5 and 33 kDa. The structural accuracy was assessed by atomic coordinate RMSD values from the reference structures of the proteins. In addition, we monitored also the number of assigned NOESY cross peaks, the average signal sensitivity, and the chemical shift spectral overlap. We show that high resolution is equally important for proteins of every molecular size. The chemical shift spectral overlap depends strongly on the corresponding spectral digital resolution. Thus, knowing the extent of overlap can be a predictor of the resulting structural accuracy. Our results show that for every molecular size a minimal digital resolution, corresponding to the natural linewidth, needs to be achieved for obtaining the highest accuracy possible for the given protein size using state-of-the-art automated NOESY assignment and structure calculation methods