[NMR screening of potential inhibitors of Citrobacter freundii methionine].

Methionine γ-lyase [EC 4.4.1.

[Optimization of the methods for small peptide solution structure determination by NMR spectroscopy].

NMR spectroscopy was recognized as a method of protein structure determination in solution. However, determination of the conformation of small peptides, which undergo fast molecular motions, remains a challenge. This is mainly caused by impossibility to collect required quantity of the distance and dihedral angle restraints from NMR spectra.

[Interface of the interaction of the middle domain of human translation termination factor eRF1 with eukaryotic ribosomes].

Termination of translation in eukaryotes is governed by two polypeptide chain release factors. The middle (M) domain of the class 1 translation termination factor eRF1 contains the strictly conserved GGQ motif and involved in hydrolysis of the peptidyl-tRNA ester bond within the peptidyl transferase center of the large ribosome subunit. Heteronuclear NMR spectroscopy was used to map the interaction interface of the M-domain of human termination factor eRF1 with eukaryotic ribosomes.