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V P Kutyshenko

Showing results (31-40 of 45) with videos related to

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Journal of Protein Chemistry|May 2, 2001
Multidomain structure of a recombinant streptokinase. A differential scanning calorimetry studyA Beldarraín, J L López-Lacomba, V P Kutyshenko, et al.
Biochemistry|August 25, 1992
Retinol-binding protein is in the molten globule state at low pHV E Bychkova, R Berni, G L Rossi, et al.
Molekuliarnaia Biologiia|January 1, 1989
[Complete assignment of signals in 1D and 2D H-NMR spectra of a 17-member oligonucleotide, a model symmetrical analog of lambda operators]A V Kurochkin, B K Chernov, M P Kirpichnikov, et al.
Molekuliarnaia Biologiia|May 1, 1989
[Staged equilibrium of carbonic anhydrase unfolding in strong denaturants]N A Rodionova, G V Semisotnov, V P Kutyshenko, et al.
FEBS Letters|November 16, 1987
Sequential mechanism of refolding of carbonic anhydrase BG V Semisotnov, N A Rodionova, V P Kutyshenko, et al.
Protein Science : a Publication of the Protein Society|September 1, 1996
Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligandsV N Uversky, V P Kutyshenko, Protasova NYu, et al.
Biofizika|November 2, 2010
[Purification of the mitochondrial calcium uniporter from the beef heart and characterization of its properties]E N Gritsenko, V P Kutyshenko, N E-L Saris, et al.
FEMS Microbiology Letters|September 15, 1993
Instability of waves formed by motile bacteriaA B Medvinsky, M A Tsyganov, V P Kutyshenko, et al.
Redox Biology|October 6, 2018
Hydroxycobalamin catalyzes the oxidation of diethyldithiocarbamate and increases its cytotoxicity independently of copper ionsM E Solovieva, Yu V Shatalin, V V Solovyev, et al.
Biomeditsinskaia Khimiia|March 13, 2015
[NMR study of human biological fluids for detection of pathologies]P M Beskaravainy, M V Molchanov, A V Suslikov, et al.
Pageof 5

Showing results (31-40 of 45) with videos related to

Sort By:
Pageof 5
Journal of Protein Chemistry|May 2, 2001
Multidomain structure of a recombinant streptokinase. A differential scanning calorimetry studyA Beldarraín, J L López-Lacomba, V P Kutyshenko, et al.
Biochemistry|August 25, 1992
Retinol-binding protein is in the molten globule state at low pHV E Bychkova, R Berni, G L Rossi, et al.
Molekuliarnaia Biologiia|January 1, 1989
[Complete assignment of signals in 1D and 2D H-NMR spectra of a 17-member oligonucleotide, a model symmetrical analog of lambda operators]A V Kurochkin, B K Chernov, M P Kirpichnikov, et al.
Molekuliarnaia Biologiia|May 1, 1989
[Staged equilibrium of carbonic anhydrase unfolding in strong denaturants]N A Rodionova, G V Semisotnov, V P Kutyshenko, et al.
FEBS Letters|November 16, 1987
Sequential mechanism of refolding of carbonic anhydrase BG V Semisotnov, N A Rodionova, V P Kutyshenko, et al.
Protein Science : a Publication of the Protein Society|September 1, 1996
Circularly permuted dihydrofolate reductase possesses all the properties of the molten globule state, but can resume functional tertiary structure by interaction with its ligandsV N Uversky, V P Kutyshenko, Protasova NYu, et al.
Biofizika|November 2, 2010
[Purification of the mitochondrial calcium uniporter from the beef heart and characterization of its properties]E N Gritsenko, V P Kutyshenko, N E-L Saris, et al.
FEMS Microbiology Letters|September 15, 1993
Instability of waves formed by motile bacteriaA B Medvinsky, M A Tsyganov, V P Kutyshenko, et al.
Redox Biology|October 6, 2018
Hydroxycobalamin catalyzes the oxidation of diethyldithiocarbamate and increases its cytotoxicity independently of copper ionsM E Solovieva, Yu V Shatalin, V V Solovyev, et al.
Biomeditsinskaia Khimiia|March 13, 2015
[NMR study of human biological fluids for detection of pathologies]P M Beskaravainy, M V Molchanov, A V Suslikov, et al.
Pageof 5