Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Farida Kh. Karataeva"'
Autor:
Ilya A. Khodov, Guzel S. Musabirova, Vladimir V. Klochkov, Farida Kh. Karataeva, Daniel Huster, Holger A. Scheidt
Publikováno v:
Journal of Molecular Liquids. 367:120502
Autor:
A. A. Balandina, Farida Kh. Karataeva, Vladimir V. Klochkov, Yu. G. Shtyrlin, L. F. Galiullina, I. Z. Rakhmatullin
Publikováno v:
BioNanoScience. 8:963-970
In the last decade, pyridoxine derivatives were widely used for the synthesis of molecules with important biological and physical properties. However, rational synthesis of the compounds with desirable biochemical or physical properties often require
Autor:
R. M. Aminova, Farida Kh. Karataeva, S.V. Efimov, Ekaterina V. Mironova, Vladimir F. Mironov, Vladimir V. Klochkov, Mudaris N. Dimukhametov, Dmitry B. Krivolapov
Publikováno v:
The Journal of Organic Chemistry. 81:5837-5850
Interaction of 4,5-dimethyl-2-(2-oxo-1,2-diphenyl)ethoxy-1,3,2-dioxaphospholane, bearing a carboxyl group in the γ-position with respect to the phosphorus atom and obtained from d,l-butanediol, with hexafluoroacetone (CCl4, -40 °C) leads to the sim
Publikováno v:
BioNanoScience. 7:555-557
New pyridoxine derivative with multiple chemical exchanges was studied by 13C (at 298 K, 188 K) and 2D NMR (1H-13C HSQC, 1H-13C HMBC) spectroscopy in acetone-d6 solution. Complete 13C NMR data (table with chemical shifts at different temperatures) is
Autor:
Farida Kh. Karataeva, Andrei Filippov, Dmitriy S. Blokhin, Adeliya R. Fayzullina, Vladimir V. Klochkov
Publikováno v:
Journal of Molecular Structure. 1102:91-94
Fibrinopeptide B (GluFib) is one of the factors of thrombosis. Normal blood protein soluble, fibrinogen (fibrinopeptide A and fibrinopeptide B), is transformed into the insoluble, fibrin, which in the form of filaments adheres to the vessel wall at t
Autor:
Konstantin S. Usachev, Dmitriy S. Blokhin, Farida Kh. Karataeva, Vladimir V. Klochkov, Rustam Abdrakhmanov
Publikováno v:
BioNanoScience. 7:204-206
In this paper, binding of Mn2+ ions to the fragment of beta-amyloid peptide (Aβ13-23) was studied. Manganese complexation induces important structural changes within the C-terminal segment of the peptide. Investigation of peptide–metal ion binding