Zobrazeno 1 - 8
of 8
pro vyhledávání: '"A G, Biktashev"'
Autor:
Olga V. Stepanenko, Irina M. Kuznetsova, Olga I. Povarova, Konstantin K. Turoverov, Olesia V. Stepanenko, Mikhail M. Shavlovsky, Vladislav V. Verkhusha, Alexander G. Biktashev
Publikováno v:
Biochemistry. 41:13127-13132
The kinetics of actin unfolding induced by guanidine hydrochloride of different concentrations was studied. The parametric representation of the kinetic dependencies of tryptophan fluorescence intensity changes recorded at two wavelengths allowed us
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4c2473a9bd1d2c0b6627006b43259844
https://doi.org/10.1021/bi026412x
https://doi.org/10.1021/bi026412x
Autor:
Vladimir N. Uversky, Irina M. Kuznetsova, Alexander G. Biktashev, Lubov' N. Malova, Natalia A. Bushmarina, Konstantin K. Turoverov
Publikováno v:
Protein & Peptide Letters. 7:411-420
Abstract: Packing density and other properties of the microenvironment of tryptophan residues in hen egg-white lysozyme macromolecule have been studied on the basis of the known 3D structure of this protein. Results presented here suggest that the ef
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9be2cbc00642b612b4b4d3afecc20760
https://doi.org/10.2174/092986650706221208100119
https://doi.org/10.2174/092986650706221208100119
Publikováno v:
Chembiochem : a European journal of chemical biology. 2(11)
GdmCl-, urea-, and pH-induced unfolding pathways of bovine carbonic anhydrase II have been analyzed by using changes induced by different denaturing agents in intensity, anisotropy, life time, and parameter A value of intrinsic fluorescence as well a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2beaa62563e1ec8d754c159ea96cfc1f
https://pubmed.ncbi.nlm.nih.gov/11948867
https://pubmed.ncbi.nlm.nih.gov/11948867
Autor:
Alexander G. Biktashev, Konstantin K. Turoverov, Vladislav V. Verkhusha, Olga I. Povarova, Irina M. Kuznetsova, Mikhail M. Shavlovsky
Publikováno v:
Biochemistry. 41(3)
The kinetics of actin unfolding induced by guanidine hydrochloride has been studied. On the basis of obtained experimental data a new kinetic pathway of actin unfolding was proposed. We have shown that the transition from native to inactivated actin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de6700c62d7dc851f43a9522caed7762
https://pubmed.ncbi.nlm.nih.gov/11790125
https://pubmed.ncbi.nlm.nih.gov/11790125
Autor:
Vladimir N. Uversky, Irina M. Kuznetsova, Konstantin K. Turoverov, Sofia Khaitlina, Alexander G. Biktashev, Konstantin S. Vassilenko
Publikováno v:
Biophysical journal. 77(5)
The propensity to associate or aggregate is one of the characteristic properties of many nonnative proteins. The aggregation of proteins is responsible for a number of human diseases and is a significant problem in biotechnology. Despite this, little
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a47cc3186f0fe3bd5975b27ce101c87
https://pubmed.ncbi.nlm.nih.gov/10545377
https://pubmed.ncbi.nlm.nih.gov/10545377
Publikováno v:
Biochemistry. 38(19)
Steady-state and time-resolved intrinsic fluorescence, fluorescence quenching by acrylamide, and surface testing by hydrophobic label ANS were used to study the structure of inactivated alpha-actin. The results are discussed together with that of ear
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::be4a37a5e474fda5b4025b6edc673eda
https://pubmed.ncbi.nlm.nih.gov/10320355
https://pubmed.ncbi.nlm.nih.gov/10320355
Publikováno v:
Tsitologiia. 40(8-9)
A description of instruments for investigation of spectral, polarizational and kinetic characteristics of fluorescence that have been designed and constructed, and are in operation at the Institute of Cytology is presented. The spectrofluorimeter wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9e3ac2e54128e2b0adb1b0f6aab1b3bb
https://pubmed.ncbi.nlm.nih.gov/9821253
https://pubmed.ncbi.nlm.nih.gov/9821253
Autor:
Alexander G. Biktashev, Natalia A. Bushmarina, Vladimir N. Uversky, Konstantin K. Turoverov, Irina M. Kuznetsova
Publikováno v:
ChemBioChem. 2:813
GdmCl-, urea-, and pH-induced unfolding pathways of bovine carbonic anhydrase II have been analyzed by using changes induced by different denaturing agents in intensity, anisotropy, life time, and parameter A value of intrinsic fluorescence as well a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f04bd44cc034eff7cfa14b164a9c8a3
https://doi.org/10.1002/1439-7633(20011105)2:11<813::aid-cbic813>3.0.co
https://doi.org/10.1002/1439-7633(20011105)2:11<813::aid-cbic813>3.0.co