MODELING THE STACKING INTERACTIONS OF FLAVIN-MONONUCLEOTIDE WITH THE NITROGENOUS BASES OF DNA
Rubrics: MODELLING IN BIOPHYCIS
Authors:
1.
Sevastopol State Univercity
Type:
Article
Pages:
from 320
to 326
Status:
Published
Received:
20.06.2018
Accepted:
20.06.2018
Published:
25.06.2018
Subject area:
UDK 577 Материальные основы жизни. Биохимия. Молекулярная биология.Биофизика
Language:
Russian
Keywords:
flavin-mononucleotide, bases DNK, semi- and nonempirical methods, dispersion interaction, intercalation
Abstract (English):
The mechanism of the interaction flavin-mononucleotide (FMN) with bases DNA and with fragment DNA were explored. The most probable structures complex FMN with bases, with pair of the bases and with fragment DNA have been calculated by means of semi- and nonempirical methods. Structures and thermodynamic parameters of complex FMN with pair of the bases DNA have been determined. The contribution of different physical-chemical forces of the interaction in stabilization complexes of molecules has been installed. Сonclusion about molecular mechanism of the interaction FMN with bases DNA has been made.
The mechanism of the interaction flavin-mononucleotide (FMN) with bases DNA and with fragment DNA were explored. The most probable structures complex FMN with bases, with pair of the bases and with fragment DNA have been calculated by means of semi- and nonempirical methods. Structures and thermodynamic parameters of complex FMN with pair of the bases DNA have been determined. The contribution of different physical-chemical forces of the interaction in stabilization complexes of molecules has been installed. Сonclusion about molecular mechanism of the interaction FMN with bases DNA has been made.
Keywords:
flavin-mononucleotide, bases DNK, semi- and nonempirical methods, dispersion interaction, intercalation
flavin-mononucleotide, bases DNK, semi- and nonempirical methods, dispersion interaction, intercalation
1. Davies D.B., Veselkov D.A., Djimant L.N., Veselkov A.N. Hetero-association of caffeine and aromatic drugs and their competitive binding with a DNA oligomer. Eur. Biophys. J., 2001, vol. 30, pp. 354-366.
2. Lubas B., Soltysik M. Proton NMR study of the interaction of riboflavin with the egg-yolk apoprotein. FEBS Letters., 1977, vol. 79, no. 1, pp. 179-182.
3. Monaco H.L. Crystal structure of chicken riboflavin-binding protein. EMBO J., 1997, vol. 16, no. 7, pp. 1475-1483.
