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V E Bychkova

Showing results (11-20 of 29) with videos related to

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Biochemistry. Biokhimiia|March 10, 2015
How membrane surface affects protein structureV E Bychkova, L V Basova, V A Balobanov
The Journal of Biological Chemistry|August 19, 2000
Multisite fluorescence in proteins with multiple tryptophan residues. Apomyoglobin natural variants and site-directed mutantsO Tcherkasskaya, V E Bychkova, V N Uversky, et al.
FEBS Letters|February 15, 1993
Mechanism of pH-induced release of retinol from retinol-binding proteinO B Ptitsyn, G Zanotti, A L Denesyuk, et al.
International Journal of Biological Macromolecules|August 1, 1991
Solvent dependence of dimensions of unfolded protein chainsG Damaschun, H Damaschun, K Gast, et al.
Biochemistry. Biokhimiia|March 17, 2018
The Molten Globule Concept: 45 Years LaterV E Bychkova, G V Semisotnov, V A Balobanov, et al.
Biochemistry. Biokhimiia|June 12, 2017
Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram?V A Balobanov, N S Katina, A V Finkelstein, et al.
Molekuliarnaia Biologiia|December 20, 2005
[Investigation of folding/unfolding kinetics of apomyoglobin]E N Baryshnikova, B S Mel'nik, G V Semisotnov, et al.
Molekuliarnaia Biologiia|May 6, 2004
[Conformational status of apomyoglobin in the presence of phospholipid vesicles at neutral pH]L V Basov, E I Tiktopulo, I A Kashparov, et al.
Folding & Design|August 26, 1998
Release of retinol and denaturation of its plasma carrier, retinol-binding proteinV E Bychkova, A E Dujsekina, A Fantuzzi, 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.
Pageof 3

Showing results (11-20 of 29) with videos related to

Sort By:
Pageof 3
Biochemistry. Biokhimiia|March 10, 2015
How membrane surface affects protein structureV E Bychkova, L V Basova, V A Balobanov
The Journal of Biological Chemistry|August 19, 2000
Multisite fluorescence in proteins with multiple tryptophan residues. Apomyoglobin natural variants and site-directed mutantsO Tcherkasskaya, V E Bychkova, V N Uversky, et al.
FEBS Letters|February 15, 1993
Mechanism of pH-induced release of retinol from retinol-binding proteinO B Ptitsyn, G Zanotti, A L Denesyuk, et al.
International Journal of Biological Macromolecules|August 1, 1991
Solvent dependence of dimensions of unfolded protein chainsG Damaschun, H Damaschun, K Gast, et al.
Biochemistry. Biokhimiia|March 17, 2018
The Molten Globule Concept: 45 Years LaterV E Bychkova, G V Semisotnov, V A Balobanov, et al.
Biochemistry. Biokhimiia|June 12, 2017
Intermediate States of Apomyoglobin: Are They Parts of the Same Area of Conformations Diagram?V A Balobanov, N S Katina, A V Finkelstein, et al.
Molekuliarnaia Biologiia|December 20, 2005
[Investigation of folding/unfolding kinetics of apomyoglobin]E N Baryshnikova, B S Mel'nik, G V Semisotnov, et al.
Molekuliarnaia Biologiia|May 6, 2004
[Conformational status of apomyoglobin in the presence of phospholipid vesicles at neutral pH]L V Basov, E I Tiktopulo, I A Kashparov, et al.
Folding & Design|August 26, 1998
Release of retinol and denaturation of its plasma carrier, retinol-binding proteinV E Bychkova, A E Dujsekina, A Fantuzzi, 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.
Pageof 3