Zobrazeno 1 - 10
of 42
pro vyhledávání: '"E I, Tiktopulo"'
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1794:1151-1158
Scanning microcalorimetry has been used to study heat denaturation of small es, Cyrillicollagen at high pressure. It has been demonstrated that an increase of the pressure by 200 MPa enlarges the structure stability by 6.8 degrees C. The pressure inc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5dcf314a4b7c839c4d1af85a9b2e819d
https://doi.org/10.1016/j.bbapap.2009.04.005
https://doi.org/10.1016/j.bbapap.2009.04.005
Autor:
N. G. Koretskaya, V.D. Vasiliev, N. V. Kiseleva, Bogdan S. Melnik, S. A. Potekhin, E. I. Tiktopulo
Publikováno v:
Biophysics. 54:143-151
Circular dichroism, scanning microcalorimetry, electron microscopy, and proteolysis were used to study the ability of wild-type δ-endotoxin Cry3A and its three mutant forms with cysteine substitutions in helices α3 and α4 (domain I) to produce oli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a22e8e8b9a72d244a5f6c03836080949
https://doi.org/10.1134/s0006350909020043
https://doi.org/10.1134/s0006350909020043
Autor:
E. I. Tiktopulo, Dmitry A. Dolgikh, Ekaterina Samatova, A. E. Dyuysekina, Vitaly A. Balobanov, V. E. Bychkova
Publikováno v:
Biochemistry (Moscow). 73:693-701
A number of residues in globins family are well conserved but are not directly involved in the primary oxygen-carrying function of these proteins. A possible role for these conserved, non-functional residues has been suggested in promoting a rapid an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e37bbdb0826cce41a3efea38de0a5b15
https://doi.org/10.1134/s0006297908060102
https://doi.org/10.1134/s0006297908060102
Publikováno v:
Biophysics. 52:489-497
Reviewed are works concerning the mechanisms of collagen (type I) fibril packing and the influence of macromolecular structure and physicochemical parameters of the medium on the process.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f231373e27a94e0bfc9e3ace264d8ede
https://doi.org/10.1134/s0006350907050065
https://doi.org/10.1134/s0006350907050065
Autor:
Anna V. El'skaya, Boris Negrutskii, I. N. Serdyuk, E. I. Tiktopulo, A. V. Novosylna, A. A. Timchenko
Publikováno v:
Biopolymers and Cell. 23:386-390
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a2b2a55b861627b535c16d942c156f64
https://doi.org/10.7124/bc.000777
https://doi.org/10.7124/bc.000777
Publikováno v:
Biophysics. 52:191-195
Analysis of the results of calorimetric study of reconstituted collagen (type I) fibrils, in particular, the half-width of the temperature transition, shows that the collagen packing density in the fibrils and the size of cooperative blocks therein d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1f2e509203f4fc3b75f9acb69b691232
https://doi.org/10.1134/s000635090702008x
https://doi.org/10.1134/s000635090702008x
Autor:
Alexander S. Spirin, Vyacheslav M. Shiryaev, S. A. Potekhin, E. I. Tiktopulo, Olga M. Selivanova
Publikováno v:
Journal of Biological Chemistry. 278:36311-36314
Ribosomal protein S1 of Thermus thermophilus overexpressed in Escherichia coli cells has been isolated and subjected to studies by analytical sedimentation and differential scanning microcalorimetry techniques. It has been demonstrated that the prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2c690475ee07b9bde7e091145ce99dd2
https://doi.org/10.1074/jbc.m304713200
https://doi.org/10.1074/jbc.m304713200
Publikováno v:
Journal of Thermal Analysis and Calorimetry. 62:153-160
The paper describes the design and the principle of operation of the differential scanning microcalorimeter SCAL-1. This instrument serves to measure thermal parameters of protein or biopolymer solutions of low concentration (from0.1 mg ml−1) in th
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::48ec4de66146fc4853eb4489e336d374
https://doi.org/10.1023/a:1010171013669
https://doi.org/10.1023/a:1010171013669
Publikováno v:
Biophysics. 54:683-685
The data on the effect of temperature on the kinetics of collagen fibril formation at physiological pH values and ionic strength in the temperature range 26–39°C have been analyzed. The temperature of 35°C optimal for collagen fibril formation ha
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::282bfdcc15210b5fe0c63d6a41b8e5f4
https://doi.org/10.1134/s0006350909060049
https://doi.org/10.1134/s0006350909060049
Autor:
E. I. Tiktopulo, Andrey V. Kajava
Publikováno v:
Biochemistry. 37:8147-8152
Thermal transitions of type I collagen fibrils were investigated by differential scanning calorimetry and spectrophotometry of turbidity within a wide range of external conditions. The advanced microcalorimeter allowed us to carry out the measurement
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c8724932c38b417ac1bedc6a767dd137
https://doi.org/10.1021/bi980360n
https://doi.org/10.1021/bi980360n