NMR structural analysis

NMR spectroscopy is unique structural-analytic method for structure elucidation and provides information about constitution, configuration and also conformation of studied compound. Our research is focused on structural study of both synthetic compound originating in laboratories of the IOCB and isolated from natural sources. We utilize modern one and multidimensional NMR techniques and obtained structural parameters are subsequently used for structure elucidation of nucleosides, nucleotides, peptides, steroids, saccharides, pheromones, helicenes and other classes of compounds.

Absolute configuration

Chirality is important property of many biologically significant compounds and knowledge of absolute configuration is necessary for structure-activity relationship evaluation. NMR enables determination of enantiomeric purity, enantiomeric excess and absolute configuration using chiral shift reagents and chiral derivatizing reagents for in-situ reactions in NMR tubes.

Thermodynamics and kinetics of chemical reactions

Our research is also focused on study of nonbonding interactions of supramolecular systems, mechanism and kinetics of deuterium exchange of pyrimidine C(5)-H using NMR and ab initio quantum chemical calculations.

Quantum chemical calculations of NMR parameters

Quantum chemical calculations of NMR parameters (shielding tensors and indirect nuclear spin-spin coupling constants) are found to be useful for prediction and interpretation of experimental NMR data. Our research is focused on calculation of these NMR parameters using ab initio methods for model compounds (peptides, nucleotides) and understanding and explanation of relationships between structural factors and calculated NMR parameters.

Molecular spectroscopy

The research is oriented towards studies of molecular conformation, assignment of absolute configuration and investigation of molecular dynamics.

We concentrate on the studies of

  • interaction of disulfide groups in proteins and peptides
  • modeling of peptides interacting with model membranes
  • protein folding
  • interaction of ligands with biomolecules

Colaboration with the IOCB teams

  • Optical activity of helicene and heterohelicene systems and their bioaplication
  • Production and characterization of active recombinant human ameloblastin
  • Molecular mechanisms of autocatalytic RTX protein FrpC from Neisseria meningitidis
  • Study of chemical structure of yeast Candida albicans