Search Results - "Kutyshenko, V. P."

Hydroxycobalamin catalyzes the oxidation of diethyldithiocarbamate and increases its cytotoxicity independently of copper ions by Solovieva, M E, Shatalin, Yu V, Solovyev, V V, Sazonov, A V, Kutyshenko, V P, Akatov, V S

“…It is known that some metals (Cu, Zn, Cd, Au) markedly increase the toxic effect of thiocarbamates. It was shown in the present study that hydroxycobalamin (a…”
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Retinol-binding protein is in the molten globule state at low pH by Bychkova, V. E, Berni, Rodolfo, Rossi, Gian Luigi, Kutyshenko, V. P, Ptitsyn, O. B

“…Using far- and near-UV circular dichroism, viscosity, tryptophan fluorescence, NMR spectra, binding of a hydrophobic probe, and microcalorimetry, we have shown…”
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NMR structure and dynamics of the chimeric protein SH3-F2 by Kutyshenko, V. P, Gushchina, L. V, Khristoforov, V. S, Prokhorov, D. A, Timchenko, M. A, Kudrevatykh, Yu. A, Fedyukina, D. V, Filimonov, V. V

“…In order to further elucidate structural and dynamic principles of protein self-organization and protein-ligand interactions, a new chimeric protein was…”
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Thermodynamic study of the apomyoglobin structure by Griko, Y V, Privalov, P L, Venyaminov, S Y, Kutyshenko, V P

“…Sperm whale apomyoglobin has been studied thermodynamically in solutions with different pH and temperature by scanning microcalorimetry, viscosimetry, nuclear…”
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Water–protein interactions in the molten-globule state of carbonic anhydrase b: An NMR spin-diffusion study by KUTYSHENKO, VICTOR P., CORTIJO, MANUEL

“…We have used the homonuclear Overhauser effect (NOE) to characterize a model protein: carbonic anhydrase B. We have obtained NOE difference spectra for this…”
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Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligands by Uversky, Vladimir N., Protasova, Natalya YU, Rogov, Vladimir V., Vassilenko, Konstantin S., Gudkov, Anatoly T., Kutyshenko, Viktor P.

“…It is obvious that functional activity of a protein molecule is closely related to its structure. On the other hand, the understanding of structure‐function…”
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Cold denaturation of myoglobin by Privalov, P L, Griko YuV, Venyaminov SYu, Kutyshenko, V P

“…The stability of the structure of sperm whale metmyoglobin has been studied in various solutions, in the temperature range -8 degrees C to 100 degrees C, by…”
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Differences in the processes of beta-lactoglobulin cold and heat denaturations by Griko YuV, Kutyshenko, V.P.

“…The changes in beta-lactoglobulin upon cold and heat denaturation were studied by scanning calorimetry, CD, and NMR spectroscopy. It is shown that, in the…”
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A Study of Water-Protein Interactions by High-Resolution NMR Spectroscopy by Kutyshenko, V P

“…The interaction between carbonic anhydrase B in the molten globule state and water molecules was studied by high-resolution NMR spectroscopy. NMR spin…”
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Guanidine Hydrochloride Unfolding of a Carbonic Anhydrase Molten Globule by Kutyshenko, V. P., Prokhorov, D. A.

“…Guanidine hydrochloride-induced unfolding of a carbonic anhydrase molten globule was studied by high-resolution nuclear magnetic resonance spectroscopy. The…”
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Sequential mechanism of refolding of carbonic anhydrase B by Semisotnov, Gennady V., Rodionova, Natalya A., Kutyshenko, Victor P., Ebert, Bernd, Blanck, Jürgen, Ptitsyn, Oleg B.

“…The kinetics of refolding of bovine carbonic anhydrase B was studied by a variety of methods over a wide range of times (from milliseconds to hours). It has…”
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A study of interactions of carbonic anhydrase B with water and urea. I. Spin-diffusion parameters that determine individual and cooperative properties of molecules by Kutyshenko, V P, Prokhorov, D A, Khristoforov, V S

“…The rigidity parameter (G), which is characteristic of protein compactness, was studied in native globular carbonic anhydrase B. The dependence of parameter G…”
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Studies of interactions of carbonic anhydrase B with water and urea: II. Spin diffusion of associates of protein intermediate state at 4.2 M of urea by Kutyshenko, V P, Prokhorov, D A, Khristoforov, V S

“…The formation of carbonic anhydrase B associates (pH 5.7, urea concentration 4.2 M, 297 K) was studied as a function of protein concentration and time by…”
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Carbonic Anhydrase B Interactions with Water and Urea by Prokhorov, D. A., Kutyshenko, V. P., Khristoforov, V. S.

“…High-resolution NMR spectroscopy has been used to study native carbonic anhydrase B unfolding with urea at pH 5.75 and T = 298 K. The rigidity parameter…”
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From fragments to morphogenesis: NMR spectroscopy of metabolites in the apex of the roots of onion by Molchanov, M. V., Kutyshenko, V. P., Budantsev, A. Yu, Ivanitsky, G. R.

“…Investigation of the mechanisms of morphogenesis is one of the central problems of biology. In order to correctly formulate a solution to this problem, it is…”
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The NMR study of human biological fluids for detection of pathologies NMR study of biological fluids by Beskaravainy, P. M., Molchanov, M. V., Suslikov, A. V., Paskevich, S. I., Kutyshenko, V. P., Vorob’ev, S. I.

“…The paper deals with the NMR spectra obtained using preparations of five different human biological body fluids. Characteristic metabolite signals of blood,…”
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Redox Reactions in Chromium-Containing Fixatives for Biological Materials by Budantsev, A. Yu, Kutyshenko, V. P.

“…—A study of redox reaction kinetics in chromium-containing fixatives (mixtures of chromic acid, bichromate, formaldehyde, and acetic acid) showed that these…”
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A study of the composition of organic substances in early mouse embryos by proton magnetic resonance by Kutyshenko, V. P., Sviridova-Chailakhyan, T. A., Stepanov, A. A., Chailakhyan, L. M.

“…A study examined the composition of organic substances present in mouse embryonic cells at early stages of preimplantation development by high-resolution…”
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Two-stage thermal unfolding of [Cys 55]-substituted Cro repressor of bacteriophage λ by Gitelson, G.I., Griko, Yu.V., Kurochkin, A.V., Rogov, V.V., Kutyshenko, V.P., Kirpichnikov, M.P., Privalov, P.L.

“…It has been shown by scanning calorimetry and 1H NMR spectroscopy that thermal denaturation of mutant λ phage cro repressor in which Val 55 was substituted for…”
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Chimeric SHA-D domain “SH3-Bergerac“: 3D structure and dynamics studies by Khristoforov, V. S, Prokhorov, D. A, Timchenko, M. A, Kudrevatykh, Yu. A, Gushchina, L. V, Filimonov, V. V, Kutyshenko, V. P

“…Protein SHA-D of the SH3-Bergerac chimeric proteins family was constructed by the substitution of the β-turn N47-D48 in the spectrin SH3 domain by the…”
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