Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

E I Tiktopulo

Showing results (21-30 of 32) with videos related to

Pageof 4
Sort By:
Biofizika|October 29, 2008
[On the mechanisms of the influence of imino acids on the physical characteristics of collagens]M A Rubin, E I Tiktopulo, V A Namiot, et al.
Molekuliarnaia Biologiia|October 24, 2002
[Conformational states of the water-soluble fragment of cytochrome b5. I. pH-induced denaturation]L V Basova, N B Il'ina, K S Vasilenko, et al.
Journal of Molecular Biology|February 20, 1989
Heat capacity and conformation of proteins in the denatured stateP L Privalov, E I Tiktopulo, Venyaminov SYu, et al.
Biochemistry|May 14, 1996
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surfaceV E Bychkova, A E Dujsekina, S I Klenin, et al.
Biofizika|May 1, 2009
[Structural changes in wild-type Cry3A delta-endotoxin and its mutants in ethyl alcohol solutions at pH 2-2.5]E I Tiktopulo, N V Kiseleva, B S Mel'nik, et al.
Biofizika|March 12, 2005
[Structural changes in Cry3A delta-endotoxin from Bacillus thuringiensis var. Tenebrionis in alcohol solutions at pH 2.0]E I Tiktopulo, N V Kiseleva, V D Vasil'ev, et al.
Biochemistry|November 21, 2001
Structure of Cry3A delta-endotoxin within phospholipid membranesO I Loseva, E I Tiktopulo, V D Vasiliev, 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.
European Journal of Biochemistry|February 1, 1982
The central tryptic fragment of histones H1 and H5 is a fully compacted domain and is the only folded region in the polypeptide chain. A thermodynamic studyE I Tiktopulo, P L Privalov, T I Odintsova, et al.
Biofizika|August 14, 1998
[Effect of a biologically active interferon fragment on the structure of the synthetic protein carrier]I Iu Afasizheva, D A Dolgikh, Z Kh Abdullaev, et al.
Pageof 4

Showing results (21-30 of 32) with videos related to

Sort By:
Pageof 4
Biofizika|October 29, 2008
[On the mechanisms of the influence of imino acids on the physical characteristics of collagens]M A Rubin, E I Tiktopulo, V A Namiot, et al.
Molekuliarnaia Biologiia|October 24, 2002
[Conformational states of the water-soluble fragment of cytochrome b5. I. pH-induced denaturation]L V Basova, N B Il'ina, K S Vasilenko, et al.
Journal of Molecular Biology|February 20, 1989
Heat capacity and conformation of proteins in the denatured stateP L Privalov, E I Tiktopulo, Venyaminov SYu, et al.
Biochemistry|May 14, 1996
Molten globule-like state of cytochrome c under conditions simulating those near the membrane surfaceV E Bychkova, A E Dujsekina, S I Klenin, et al.
Biofizika|May 1, 2009
[Structural changes in wild-type Cry3A delta-endotoxin and its mutants in ethyl alcohol solutions at pH 2-2.5]E I Tiktopulo, N V Kiseleva, B S Mel'nik, et al.
Biofizika|March 12, 2005
[Structural changes in Cry3A delta-endotoxin from Bacillus thuringiensis var. Tenebrionis in alcohol solutions at pH 2.0]E I Tiktopulo, N V Kiseleva, V D Vasil'ev, et al.
Biochemistry|November 21, 2001
Structure of Cry3A delta-endotoxin within phospholipid membranesO I Loseva, E I Tiktopulo, V D Vasiliev, 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.
European Journal of Biochemistry|February 1, 1982
The central tryptic fragment of histones H1 and H5 is a fully compacted domain and is the only folded region in the polypeptide chain. A thermodynamic studyE I Tiktopulo, P L Privalov, T I Odintsova, et al.
Biofizika|August 14, 1998
[Effect of a biologically active interferon fragment on the structure of the synthetic protein carrier]I Iu Afasizheva, D A Dolgikh, Z Kh Abdullaev, et al.
Pageof 4