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V A Balobanov

Showing results (1-10 of 8) 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
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.
Biochemistry. Biokhimiia|June 7, 2011
Apomyoglobin mutants with single point mutations at val10 can form amyloid structures at permissive temperatureN S Katina, N B Ilyina, I A Kashparov, et al.
Molekuliarnaia Biologiia|September 29, 2010
[Kinetics of interaction between apomyoglobin and phospholipid membrane]V A Balobanov, N B Il'ina, N S Katina, et al.
Biochemistry. Biokhimiia|June 23, 2020
Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable FragmentS Yu Grishin, U F Dzhus, O M Selivanova, et al.
Biochemistry. Biokhimiia|July 16, 2008
pH-induced equilibrium unfolding of apomyoglobin: substitutions at conserved Trp14 and Met131 and non-conserved Val17 positionsA E Dyuysekina, D A Dolgikh, E N Samatova Baryshnikova, et al.
Molekuliarnaia Biologiia|October 17, 2007
[Equilibrium unfolding of mutant apomyoglobins with substitutions of conserved nonfunctional residues by alanine]E N Baryshnikova, V A Balobanov, N S Katina, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
Biochemistry. Biokhimiia|March 10, 2015
How membrane surface affects protein structureV E Bychkova, L V Basova, V A Balobanov
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.
Biochemistry. Biokhimiia|June 7, 2011
Apomyoglobin mutants with single point mutations at val10 can form amyloid structures at permissive temperatureN S Katina, N B Ilyina, I A Kashparov, et al.
Molekuliarnaia Biologiia|September 29, 2010
[Kinetics of interaction between apomyoglobin and phospholipid membrane]V A Balobanov, N B Il'ina, N S Katina, et al.
Biochemistry. Biokhimiia|June 23, 2020
Comparative Analysis of Aggregation of Thermus thermophilus Ribosomal Protein bS1 and Its Stable FragmentS Yu Grishin, U F Dzhus, O M Selivanova, et al.
Biochemistry. Biokhimiia|July 16, 2008
pH-induced equilibrium unfolding of apomyoglobin: substitutions at conserved Trp14 and Met131 and non-conserved Val17 positionsA E Dyuysekina, D A Dolgikh, E N Samatova Baryshnikova, et al.
Molekuliarnaia Biologiia|October 17, 2007
[Equilibrium unfolding of mutant apomyoglobins with substitutions of conserved nonfunctional residues by alanine]E N Baryshnikova, V A Balobanov, N S Katina, et al.
Pageof 1