Reversible Dimerization of Human Serum Albumin

Show simple item record Chubarov, Alexey Spitsyna, Anna Krumkacheva, Olesya Mitin, Dmitry Suvorov, Daniil Tormyshev, Victor Fedin, Matvey Bowman, Michael K. Bagryanskaya, Elena 2021-08-25T21:04:16Z 2021-08-25T21:04:16Z 2020
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). en_US
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.language English en_US
dc.subject human serum albumin en_US
dc.subject pulse dipole EPR en_US
dc.subject aggregation en_US
dc.title Reversible Dimerization of Human Serum Albumin en_US
dc.type text

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