Publications by authors named "N V Korolev"
Eukaryotic DNA is packaged in the cell nucleus into chromatin, composed of arrays of DNA-histone protein octamer complexes, the nucleosomes. Over the past decade, it has become clear that chromatin structure in vivo is not a hierarchy of well-organized folded nucleosome fibers but displays considerable conformational variability and heterogeneity. In vitro and in vivo studies, as well as computational modeling, have revealed that attractive nucleosome-nucleosome interaction with an essential role of nucleosome stacking defines chromatin compaction.
View Article and Find Full Text PDFBackground: Hemodialyzers should efficiently eliminate small and middle molecular uremic toxins and possess exceptional hemocompatibility to improve well-being of patients with end-stage kidney disease. However, performance and hemocompatibility get compromised during treatment due to adsorption of plasma proteins to the dialyzer membrane. Increased membrane hydrophilicity reduces protein adsorption to the membrane and was implemented in the novel FX CorAL dialyzer.
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- DNA behaves as a highly charged polyelectrolyte, undergoing phase separation influenced by multivalent cations and other charged species, leading to processes like DNA condensation and the formation of liquid crystalline structures.
- DNA in the cell nucleus is organized into chromatin around histones, creating nucleosomes, while recent studies highlight how biomolecular condensates form through liquid-liquid phase separation (LLPS), playing a key role in cell compartmentalization.
- The review explores DNA and chromatin LLPS from a colloidal physical chemistry perspective, comparing traditional phase separation in the presence of cations and surfactants with the dynamic droplet formation observed in DNA-protein interactions.
Telomere repeat binding factor 2 (TRF2) is an essential component of the telomeres and also plays an important role in a number of other non-telomeric processes. Detailed knowledge of the binding and interaction of TRF2 with telomeric nucleosomes is limited. Here, we study the binding of TRF2 to in vitro-reconstituted kilobasepair-long human telomeric chromatin fibres using electron microscopy, single-molecule force spectroscopy and analytical ultracentrifugation sedimentation velocity.
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- To understand chromatin folding and genomic activities, multiscale models are necessary due to the complex structures within the cell nucleus.
- This study focuses on the nucleosome core particle (NCP) aggregates and examines their interactions using bottom-up multiscale coarse-grained simulations along with all-atom MD simulations.
- The findings reveal how different concentrations of multivalent cations like Mg(HO) and CoHex influence NCP aggregation patterns, providing valuable insights into chromatin structure and dynamics.