For the recent 20 years I've been working in the N.D. Zelinsky Institute of Organic Chemistry NMR center as glycopolymer structural researcher in the group of Prof. Knirel (partly as a phd student supervised by Prof. Shashkov). Our systematic chemical and immunochemical studies are aimed at correlation between the O-antigen structure and the immunospecificity of strains, which is important for obtaining synthetic diagnosticums, vaccines and immunostimulators.

Besedes a bacterial class on which I focused in 1996-2002 (Proteus studies), a lot of other bacterial O-antigens were investigated (see below).

The other projects whichg I participated or carried out personally:

• Development of the algorithm, software and databases ("BIOPSEL") for the automated prediction of glycopolymer primary structure based on ¹³Ñ NMR data (2000-2005, PhD thesis in 2001).
• Strict modeling of bacterial cell wall peptidoglycan tertiary structure (2003-2004), funded by Research Center Borstel.
• Development of structural, taxonomical and bibliographical database of bacterial carbohydrates ("BCSDB", 2005-now), funded by International Science and technology Center, Russian president science support program and Russian Foundation for Basic Research.
• NMR studies of other compounds than glycopolymers and glycoconjugates (metalo-organic complexes, bacteriopurpurin derivatives, small organic molecules hydrazone isomerism etc.)

Glyco-studies included the elucidation of structure of natural glycopolymers and glycoconjugates by NMR spectroscopic methods. Click here to view the approximate plan of a glycopolymer NMR investigation. The NMR experiments were carried out on Bruker NMR instruments (WM250, AM300, DRX500) and included the following:

NMR experiment	Its result
1D 13C NMR	preliminary data, glycosylation effects (=> substitution pattern, absolute configurations)
1D 1H NMR	HH-coupling constants analysis (=> monomeric composition, anomeric configurations)
1D 31P NMR	revealing non-sugar substituents
1D H-Gated 13C NMR	anomeric configuration, cycle sizes
1D Attached Proton Test	methylen groups assignment
2D 1H,1H COSY	vicinal proton-proton interactions (=> 1H NMR spectrum assignment)
2D 1H,1H Double Quantum Filter COSY	simplifying the COSY spectrum by the removal of diagonal line
2D H,H-relayed COSY (RCT, RCT2)	far proton-proton interactions (=> 1H NMR spectrum assignment)
2D TOtal Correlation SpectroscopY	excluding the spin system subsets (of residues) from 1H NMR spectrum
1D 1H difference mode double resonance	signal shape analysis (=> thorough 1H NMR spectrum assignment )
2D 31P,1H COSY	localization of phospho-containing substituents
2D 13C,1H COSY	direct heteronuclear coupling constants (=> 13C NMR spectrum assignment)
2D 1H,13C Heteronuclear Multiple-Quantum Coherence	direct heteronuclear coupling constants (=> 13C NMR spectrum assignment, constant measurement)
2D Heteronuclear Multiple-Bond Correlation	far heteronuclear interactions, including transglycosidic (=> residue sequence)
2D NOE SpectroscopY	revealing spatial H-H contacts in oligomers, including transglycosydic (=> substitution pattern, residue sequence)
2D Rotating frame nuclear Overhauser Effect SpectroscopY	revealing spatial H-H contacts, including transglycosydic (=> substitution pattern, residue sequence)
1D difference mode NOE spectroscopy	thorough analysis of H-H spatial contacts

Structural studies of the Proteus O-antigens were supported by more than 10 RFBR and INTAS grants (grant list here).

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