000			02422nab a2200349 c 4500
001			vtls000623209
003			RU-ToGU
005			20210906220314.0
007			cr |
008			180322|2018 ne s a eng dd
024	7		_a10.1016/j.jphotochem.2017.08.041 _2doi
035			_ato000623209
040			_aRU-ToGU _brus _cRU-ToGU
245	1	0	_aInsight into the fluorescence quenching of Trp214 at HSA by the Dimetridazole ligand from simulation _cV. A. Pomogaev, R. R. Ramazanov, K. Ruud, V. Ya. Artyukhov
504			_aБиблиогр.: 70 назв.
520	3		_aSpectroscopy is an important tool for detecting drug binding to amino acid sequences. One such important spectroscopic process is the fluorescence quenching due to charge transfer (CT) processes between a drug molecule and the chromophore center of Human Serum Albumin (HSA). We present a theoretical investigation of the CT occurring upon electronic excitation when a dimetridazole (Dmz) molecule incorporated in HSA interacts with tryptophan residue (Trp214). Structures of the donor–acceptor complexes were optimized using density-functional theory in vacuum as well as extracted from molecular dynamics (MD) trajectories of the Dmz and Trp214 complexes in HSA (Dmz&Trp214@HSA). Absorption, emission, and fluorescence quenching of the Trp214&Dmz complex in a large number of MD conformers were calculated using various quantum-mechanical approaches in order to generate statistical spectra that are then used for studying the CT between the non-bonded donor and the acceptor.
653			_aдиметридазол
653			_aмолекулярная динамика
653			_aквантовая механика
653			_aтриптофан
653			_aаминокислотная последовательность
655		4	_aстатьи в журналах _9681159
700	1		_aPomogaev, Vladimir A. _999172
700	1		_aRuud, Kenneth _9158979
700	1		_aArtyukhov, Viktor Ya. _d1942- _9101602
700	1		_aRamazanov, Ruslan R. _9158980
773	0		_tJournal of photochemistry and photobiology A: Chemistry _d2018 _gVol. 354. P. 86-100 _x1010-6030
852	4		_aRU-ToGU
856	7		_uhttp://vital.lib.tsu.ru/vital/access/manager/Repository/vtls:000623209
908			_aстатья
999			_c60959