Reversible Dimerization of Human Serum Albumin
dc.contributor.author | Chubarov, Alexey | |
dc.contributor.author | Spitsyna, Anna | |
dc.contributor.author | Krumkacheva, Olesya | |
dc.contributor.author | Mitin, Dmitry | |
dc.contributor.author | Suvorov, Daniil | |
dc.contributor.author | Tormyshev, Victor | |
dc.contributor.author | Fedin, Matvey | |
dc.contributor.author | Bowman, Michael K. | |
dc.contributor.author | Bagryanskaya, Elena | |
dc.contributor.other | Institute of Chemical Biology & Fundamental Medicine, Siberian Branch of the RAS | |
dc.contributor.other | Russian Academy of Sciences | |
dc.contributor.other | Novosibirsk State University | |
dc.contributor.other | Vorozhtsov Novosibirsk Institute of Organic Chemistry | |
dc.contributor.other | International Tomography Center, Siberian Branch of Russian Academy of Sciences | |
dc.contributor.other | University of Alabama Tuscaloosa | |
dc.date.accessioned | 2021-08-25T21:04:16Z | |
dc.date.available | 2021-08-25T21:04:16Z | |
dc.date.issued | 2020 | |
dc.description.abstract | Pulsed Dipolar Spectroscopy (PDS) methods of Electron Paramagnetic Resonance (EPR) were used to detect and characterize reversible non-covalent dimers of Human Serum Albumin (HSA), the most abundant protein in human plasma. The spin labels, MTSL and OX063, were attached to Cys-34 and these chemical modifications of Cys-34 did affect the dimerization of HSA, indicating that other post-translational modifications can modulate dimer formation. At physiologically relevant concentrations, HSA does form weak, non-covalent dimers with a well-defined structure. Dimer formation is readily reversible into monomers. Dimerization is very relevant to the role of HSA in the transport, binding, and other physiological processes. | en_US |
dc.format.mimetype | application/pdf | |
dc.identifier.citation | Chubarov, A., Spitsyna, A., Krumkacheva, O., Mitin, D., Suvorov, D., Tormyshev, V., Fedin, M., Bowman, M., Bagryanskaya, E. (2020): Reversible Dimerization of Human Serum Albumin. Molecules. 26(1). | |
dc.identifier.doi | 10.3390/molecules26010108 | |
dc.identifier.orcid | https://orcid.org/0000-0002-0777-5103 | |
dc.identifier.orcid | https://orcid.org/0000-0002-0537-5755 | |
dc.identifier.orcid | https://orcid.org/0000-0002-5708-7595 | |
dc.identifier.orcid | https://orcid.org/0000-0003-0057-383X | |
dc.identifier.orcid | https://orcid.org/0000-0003-0454-979X | |
dc.identifier.uri | http://ir.ua.edu/handle/123456789/8069 | |
dc.language | English | |
dc.language.iso | en_US | |
dc.publisher | MDPI | |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | |
dc.subject | human serum albumin | |
dc.subject | pulse dipole EPR | |
dc.subject | aggregation | |
dc.subject | DIMER | |
dc.subject | BINDING | |
dc.subject | DYNAMICS | |
dc.subject | Biochemistry & Molecular Biology | |
dc.subject | Chemistry, Multidisciplinary | |
dc.subject | Chemistry | |
dc.title | Reversible Dimerization of Human Serum Albumin | en_US |
dc.type | text | |
dc.type | Article |
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