V P Kutyshenko|S I Vorob'ev - JoVE Visualize

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Bioorganicheskaia Khimiia|November 1, 1986

[Comparative study of conformation properties of Fc-fragments of human immunoglobulin G subclasses using 1H-NMR]V S Khristoforov, V P Kutyshenko, V M Abramov, et al.

Biofizika|November 1, 1996

[The use of 1H-NMR spectroscopy for the study of cell cultures]D I Iurkevich, V P Kutyshenko, I I Selezneva, et al.

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.

Grudnaia I Serdechno-Sosudistaia Khirurgiia|January 1, 1990

[Possibilities of the use of perfluorocarbon emulsions in prolonged storage of a donor heart]S I Vorob'ev, B I Islamov, Iu V Ladilov

Eksperimental'Naia I Klinicheskaia Farmakologiia|March 1, 1992

[The effect of the surface-active substance proxanol on the ischemic myocardium]Iu V Ladilov, B I Islamov, S I Vorob'ev

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.

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Showing results (31-40 of 54) with videos related to

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Bioorganicheskaia Khimiia|November 1, 1986

[Comparative study of conformation properties of Fc-fragments of human immunoglobulin G subclasses using 1H-NMR]V S Khristoforov, V P Kutyshenko, V M Abramov, et al.

Biofizika|November 1, 1996

[The use of 1H-NMR spectroscopy for the study of cell cultures]D I Iurkevich, V P Kutyshenko, I I Selezneva, et al.

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.

Grudnaia I Serdechno-Sosudistaia Khirurgiia|January 1, 1990

[Possibilities of the use of perfluorocarbon emulsions in prolonged storage of a donor heart]S I Vorob'ev, B I Islamov, Iu V Ladilov

Eksperimental'Naia I Klinicheskaia Farmakologiia|March 1, 1992

[The effect of the surface-active substance proxanol on the ischemic myocardium]Iu V Ladilov, B I Islamov, S I Vorob'ev

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.

Pageof 6