Zobrazeno 1 - 10
of 55
pro vyhledávání: '"V E, Bychkova"'
Autor:
Vitalii A. Balobanov, Dmitry A. Dolgikh, Rita V. Chertkova, Anna Egorova, V. E. Bychkova, Mikhail P. Kirpichnikov
Publikováno v:
Biomolecules
Volume 10
Issue 2
Biomolecules, Vol 10, Iss 2, p 241 (2020)
Volume 10
Issue 2
Biomolecules, Vol 10, Iss 2, p 241 (2020)
Engineering of amyloid structures is one of the new perspective areas of protein engineering. Studying the process of amyloid formation can help find ways to manage it in the interests of medicine and biotechnology. One of the promising candidates fo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b3f172fdc9e035bff973b4b0847ade2d
Publikováno v:
The Journal of Physical Chemistry B. 122:11228-11239
Under mildly acidic conditions (pH 4-4.5) apomyoglobin (apoMb) adopts a partially structured equilibrium state ( M-state) that structurally resembles a kinetic intermediate encountered at a late stage of folding to the native structure at neutral pH.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc71bada4b29fa16b5c64dbb689f770d
https://doi.org/10.1021/acs.jpcb.8b06895
https://doi.org/10.1021/acs.jpcb.8b06895
Publikováno v:
Biochemistry (Moscow). 83:S33-S47
In this review, we describe traditional systems where the molten globule (MG) state has been detected and give a brief description of the solution of Levinthal's paradox. We discuss new results obtained for MG-mediated folding of "nontraditional" pro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5fe7e5a31b6785a0a5f924d6ad93bf83
https://doi.org/10.1134/s0006297918140043
https://doi.org/10.1134/s0006297918140043
Publikováno v:
Biochemistry. Biokhimiia. 82(5)
Several research teams have reported detection and characterization of various apomyoglobin intermediate states different in their accumulation mode, thus putting a natural question as to proportions of these intermediates. The current report present
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f70b03f75c4f498b2ad7005e6a09531
https://pubmed.ncbi.nlm.nih.gov/28601072
https://pubmed.ncbi.nlm.nih.gov/28601072
Publikováno v:
Biochemistry (Moscow). 79:1483-1514
The immediate environment of the negatively charged membrane surface is characterized by decreased dielectric constant and pH value. These conditions can be modeled by water-alcohol mixtures at moderately low pH. Several globular proteins were invest
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::029eaec9cd79e4ed620291a52c3f798b
https://doi.org/10.1134/s0006297914130045
https://doi.org/10.1134/s0006297914130045
Autor:
N. S. Katina, Victor V. Marchenkov, V. E. Bychkova, Anatoly S. Glukhov, Vitalii A. Balobanov, Nelly B. Ilyina, V.D. Vasiliev, Alexey D. Nikulin
Publikováno v:
Biophysical journal. 113(5)
Investigation of the molecular mechanisms underlying amyloid-related human diseases attracts close attention. These diseases, the number of which currently is above 40, are characterized by formation of peptide or protein aggregates containing a cros
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b29c90693e0b5d9757c3e49b18c6eebe
https://pubmed.ncbi.nlm.nih.gov/28877500
https://pubmed.ncbi.nlm.nih.gov/28877500
Autor:
A. A. Timchenko, V.D. Vasiliev, V. E. Bychkova, I. A. Kashparov, N. S. Katina, Hiroshi Kihara, Vitaly A. Balobanov
Publikováno v:
Macromolecular Symposia. :215-226
Association of protein molecules in human tissues underlies many diseases, which brings it in the focus of numerous studies. Previous reports described amyloid formation with the unfolded protein state taken as the starting point. Here, we present ki
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::253c930e6aa8036e73804075bb125739
https://doi.org/10.1002/masy.201200005
https://doi.org/10.1002/masy.201200005
Autor:
Vitaly A. Balobanov, I. A. Kashparov, V.D. Vasiliev, Nelly B. Ilyina, V. E. Bychkova, N. S. Katina
Publikováno v:
Biochemistry (Moscow). 76:555-563
Formation of amyloid-like protein aggregates in human organs and tissues underlies many serious diseases, therefore being in the focus of numerous biochemical, medical, and molecular biological studies. So far, formation of amyloids by globular prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d85029d7c277d160645f01399279507b
https://doi.org/10.1134/s0006297911050051
https://doi.org/10.1134/s0006297911050051
Autor:
N. B. Il’ina, Vitaly A. Balobanov, Dmitry A. Dolgikh, V. E. Bychkova, I. A. Kashparov, N. S. Katina
Publikováno v:
Molecular Biology. 44:624-632
The interaction of apomyoglobin and its mutant forms with phospholipid membranes was studied using tryptophan fluorescence and circular dichroism in the far UV region. It is shown that a negatively charged phospholipid membrane can have a dual effect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0b210fade9505c89a74dfac1741728c8
https://doi.org/10.1134/s0026893310040187
https://doi.org/10.1134/s0026893310040187
Autor:
V. E. Bychkova, Natalia S. Katina, Ekaterina Samatova, Dmitry A. Dolgikh, Bogdan S. Melnik, Alexei V. Finkelstein, Vitaly A. Balobanov
Publikováno v:
Protein Science. 18:2152-2159
Influence of 12 nonpolar amino acids residues from the hydrophobic core of apomyoglobin on stability of its native state and folding intermediate was studied. Six of the selected residues are from the A, G and H helices; these are conserved in struct
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::512de1de1c1d31a8a98a900bb4495907
https://doi.org/10.1002/pro.229
https://doi.org/10.1002/pro.229