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G V Semisotnov

Showing results (11-20 of 38) with videos related to

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Molekuliarnaia Biologiia|December 20, 2005
[Investigation of folding/unfolding kinetics of apomyoglobin]E N Baryshnikova, B S Mel'nik, G V Semisotnov, et al.
FEBS Letters|December 7, 1992
'All-or-none' mechanism of the molten globule unfoldingV N Uversky, G V Semisotnov, R H Pain, et al.
Journal of Molecular Biology|February 6, 1998
Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopyM Arai, T Ikura, G V Semisotnov, et al.
FEBS Letters|November 22, 1993
Secondary structure of globular proteins at the early and the final stages in protein foldingK Kuwajima, G V Semisotnov, A V Finkelstein, et al.
FEBS Letters|April 18, 2000
GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solutionA A Timchenko, B S Melnik, H Kihara, et al.
FEBS Letters|March 12, 1990
Evidence for a molten globule state as a general intermediate in protein foldingO B Ptitsyn, R H Pain, G V Semisotnov, et al.
Protein Expression and Purification|December 9, 2015
Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different originN Yu Marchenko, E V Sikorskaya, V V Marchenkov, 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|April 9, 1990
An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'M E Goldberg, G V Semisotnov, B Friguet, et al.
Bioorganicheskaia Khimiia|September 25, 1999
[Monomeric form of the molecular chaperone GroEL: structure, stability, and oligomerization]A K Surin, N V Kotova, S Iu Marchenkova, et al.
Pageof 4

Showing results (11-20 of 38) with videos related to

Sort By:
Pageof 4
Molekuliarnaia Biologiia|December 20, 2005
[Investigation of folding/unfolding kinetics of apomyoglobin]E N Baryshnikova, B S Mel'nik, G V Semisotnov, et al.
FEBS Letters|December 7, 1992
'All-or-none' mechanism of the molten globule unfoldingV N Uversky, G V Semisotnov, R H Pain, et al.
Journal of Molecular Biology|February 6, 1998
Kinetic refolding of beta-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopyM Arai, T Ikura, G V Semisotnov, et al.
FEBS Letters|November 22, 1993
Secondary structure of globular proteins at the early and the final stages in protein foldingK Kuwajima, G V Semisotnov, A V Finkelstein, et al.
FEBS Letters|April 18, 2000
GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solutionA A Timchenko, B S Melnik, H Kihara, et al.
FEBS Letters|March 12, 1990
Evidence for a molten globule state as a general intermediate in protein foldingO B Ptitsyn, R H Pain, G V Semisotnov, et al.
Protein Expression and Purification|December 9, 2015
Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different originN Yu Marchenko, E V Sikorskaya, V V Marchenkov, 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|April 9, 1990
An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'M E Goldberg, G V Semisotnov, B Friguet, et al.
Bioorganicheskaia Khimiia|September 25, 1999
[Monomeric form of the molecular chaperone GroEL: structure, stability, and oligomerization]A K Surin, N V Kotova, S Iu Marchenkova, et al.
Pageof 4