Nanoparticle-based FRET pair selection for investigation of metallothionein dimerization
Abstract
Metalloproteins (MTs) are one of the most diverse classes of proteins, with the intrinsic metal atoms providing a catalytic, regulatory and structural role crucial to protein functioning. When stored under aerobic conditions, MTs might form dimers (as well as higher oligomers) that play an essential role as mediators in oxidoreduction signalling pathways. In this work, we explore the non-oxidative dimerization process characterized by metal (Cd) bridging of MT monomers by Förster resonance energy transfer. The formation of MT dimers/oligomers was investigated by applying capillary electrophoresis and matrix-assisted laser desorption/ionization with mass spectrometric detection.
Keywords
Metallothionein, dimerization, capillary electrophoresis, Förster resonance energy transferPersistent identifier
http://hdl.handle.net/11012/196669Document type
Peer reviewedDocument version
Final PDFSource
NANOCON 2019 CONFERENCE PROCEEDINGS. 2020, p. 406-410.https://doi.org/10.37904/nanocon.2019.8566
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