Publications by authors named "Vladimir I Vorob'ev"
A computer modeling of thermodynamic properties of a long DNA of N base pairs that includes omega interstrand crosslinks (ICLs), or omega chemical modifications involving one strand (monofunctional adducts, intrastrand crosslinks) has been carried out. It is supposed in our calculation that both types of chemical modifications change the free energy of the helix-coil transition at sites of their location by deltaF. The value deltaF>0 corresponds to stabilization, i.
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- Cisplatin Binding
- : The antitumor drug cisplatin distorts DNA's double helix, initially reducing its melting temperature (Tm), but this destabilization is countered by a decrease in DNA charge density, which can increase Tm, especially at low sodium ion concentrations.
- Influence of pH
- : The impact of cisplatin on DNA stability is also affected by pH levels; at alkaline pH (10.5-10.8), the decrease in Tm is significantly heightened due to changes in base pair protonation and charge density, while at neutral pH, this effect is minimal.
- Interstrand Crosslinking
- : Although cisplatin
Article Synopsis
- Long-range interactions between ligands bound to DNA can lead to a phase transition, impacting how ligands bind to the DNA molecule.
- This binding behavior is characterized by a sharp change in the concentration of bound ligands at a specific critical concentration of free ligands.
- The study examines the necessary conditions for this phase transition, highlighting that longer ligands require stronger long-range interactions to induce the transition, and that while neighboring ligand interactions alone can’t initiate the transition, they can reduce the energy threshold needed for it.
The HMG1 ta(i)le.
J Biomol Struct Dyn
June 2002
We have studied structural changes in DNA/protein complexes using the CD spectroscopy, upon the interaction of HMG1-domains with calf thymus DNA at different ionic strengths. HMG1 protein isolated from calf thymus and recombinant HMG1-(A+B) protein were used. Recombinant protein HMG1-(A+B) represents a rat HMG1 lacking C-terminal acidic tail.
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