English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

The computer simulations of the interaction of DNA fragments and actinocin derivative (ActII) with ligand-target ratio 1:1 and 2:1 were carried out by a Monte Carlo method taking into account water environment. Low-energy molecular structures corresponding to the most probable models of two types of complexes – binding of ActII in minor groove and intercalation of ActII into GC-site with different complex stehiometry were obtained The energetic and structural parameters of the complex formation were calculated. The stability of investigated complexes was conditioned by Van der Waals and electrostatic interactions as well as by the interaction with a solvent. The water molecules contribute to the stabilization of complexes due to the formation of water bridges between donor-acceptor groups of DNA fragments and ligands. Possible sizes of ActII binding sites in the minor groove were determined. They equaled 3–4 b. p. per the ligand molecule. The sizes of binding sites of intercalating ActII molecules into GC-site are obviously bigger than 4 b. p. per the ligand molecule. The results obtained are in agreement with the experimental data.

The binding of actinocin derivative with DNA fragments (Monte Carlo simulation)