Publications by authors named "Vladimir Isaev-Ivanov"
Article Synopsis
- The study investigates the interactions of multimeric complexes formed by alpha-lactalbumin and lactoferrin with oleic acid, focusing on their potential pro-apoptotic effects in tumor cells.
- Using small-angle neutron scattering (SANS), the research reveals that alpha-lactalbumin forms complexes with polydisperse oleic acid micelles, while lactoferrin forms a uniform nanoscale particle system.
- Additionally, both complexes appear to influence chromatin structure in isolated nuclei, suggesting their role in exhibiting specific anti-tumor activities.
Article Synopsis
- New research highlights the significance of partially assembled nucleosome states (PANS) alongside traditional nucleosome structures in regulating DNA accessibility within cells.
- The study utilized molecular dynamics simulations and atomic force microscopy to construct detailed models of key PANS: hexasomes, tetrasomes, and disomes, revealing that certain DNA regions remain stable and protected when in contact with histones.
- The findings suggest that PANS are prevalent in active chromatin, possibly promoting faster transcription, and prompt new interpretations of existing experimental data related to DNA protection.
Using molecular modeling techniques we have built the full atomic structure and performed molecular dynamics simulations for the complexes formed by Escherichia coli RecX protein with a single-stranded oligonucleotide and with RecA presynaptic filament. Based on the modeling and SANS experimental data a sandwich-like filament structure formed two chains of RecX monomers bound to the opposite sides of the single stranded DNA is proposed for RecX::ssDNA complex. The model for RecX::RecA::ssDNA include RecX binding into the grove of RecA::ssDNA filament that occurs mainly via Coulomb interactions between RecX and ssDNA.
View Article and Find Full Text PDFRecA protein is a central enzyme in homologous DNA recombination, repair and other forms of DNA metabolism in bacteria. It functions as a flexible helix-shaped filament bound on stretched single-stranded or double-stranded DNA in the presence of ATP. In this work, we present an atomic level model for conformational transitions of the RecA filament.
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