We studied the interaction of chaperonin GroEL with different misfolded forms of tetrameric phosphorylating glyceraldehyde-3-phosphate dehydrogenase (GAPDH): (1) GAPDH from rabbit muscles with all SH-groups modified by 5,5Ј-dithiobis(2-nitrobenzoate); (2) O-R-type dimers of mutant GAPDH from Bacillus stearothermophilus with amino acid substitutions Y283V, D282G, and Y283V/W84F, and (3) O-Ptype dimers of mutant GAPDH from B. stearothermophilus with amino acid substitutions Y46G/S48G and Y46G/R52G. It was shown that chemically modified GAPDH and the O-R-type mutant dimers bound to GroEL with 1:1 stoichiometry and dissociation constants K d of 0.4 and 0.9 M, respectively. A striking feature of the resulting complexes with GroEL was their stability in the presence of Mg-ATP. Chemically modified GAPDH and the O-R-type mutant dimers inhibited GroEL-assisted refolding of urea-denatured wild-type GAPDH from B. stearothermophilus but did not affect its spontaneous reactivation. In contrast to the O-R-dimers, the O-P-type mutant dimers neither bound nor affected GroEL-assisted refolding of the wild-type GAPDH. Thus, we suggest that interaction of GroEL with certain types of misfolded proteins can result in the formation of stable complexes and the impairment of chaperonin activity.Keywords: GAPDH; GroEL; oligomeric proteins; refolding; denaturation; immobilization; chemical modification; protein-protein interactions Heat shock proteins (HSPs) constitute highly conserved families of proteins which play an essential role in the folding, unfolding, and transport of proteins within both prokaryotic and eukaryotic cells (Fenton and Horwich 1997). The best characterized chaperonin from Escherichia coli, GroEL, is a homo-oligomeric complex of 14 subunits which are arranged in two rings, stacked back to back (Braig et al. 1994). GroEL monomer has a molecular weight of 58 kDa and comprises three domains: an apical domain responsible for binding both substrates and co-chaperonin GroES, an equatorial domain containing an ATP-binding site, and an intermediate hinge domain. Together with GroES, GroEL captures, encapsulates, and releases its substrates in cycles driven by ATP binding and hydrolysis (Sigler et al. 1998;Rye et al. 1999). Strict GroEL-, GroES-, and ATP-dependent refolding of nonnative proteins in vitro was described for many chemically denatured proteins. However, chaperonin-mediated refolding of some proteins (i.e., enolase, tryptophanase, rhodanese, and glutamine synthetase) can take place in the presence of ADP and nonhydrolyzable ATP analogs (Mizobata et al. 1992;Kubo et al. 1993 Abbreviations: DAB, 3,5Ј-diaminobenzidine tetrahydrochloride; DTNB, 5,5Ј-dithiobis(2-nitrobenzoate); DSC, differential scanning calorimetry; DTT, dithiothreitol; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; TBS, Tris-buffered saline.Article published online ahead of print. Article and publication date are at

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Purpose At present, the development of information technologies changes the whole system of public functioning. Special attention is paid to the system of higher education, as it forms future highly qualified specialists, who will become the basis of digital economy. According to this, new remote technologies are implemented into the system of education each year, which are a basic prototype of smart technologies. The purpose of this paper is to determine the role of remote technologies in the development of the system of higher education and to form skills with the students. Design/methodology/approach Based on this, it is necessary to solve the following tasks: view the aspects, peculiarities and possibilities of remote education; distinguish the main tools of remote technologies in education; offer electronic final program as a remote method of evaluation of students’ knowledge. Findings In this study, the following methods are used: analysis, synthesis, logical method, abstraction and comparison. Scientific novelty consists in performing research in the sphere of significance and implementation of remote technologies in the system of higher education of the Russian Federation. Originality/value This research could be useful for public officers who form programs of development of higher education and for academic staff of higher educational establishments.

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The article considers the adjustment of the course design process to the new education paradigm.