FRET as a powerful tool to study protein dimerization

被引：0

作者：

Pavelicova, Kristyna ^{[1
]}

Nejdl, Lukas ^{[1
]}

Vanickova, Lucie P. ^{[1
]}

Macka, Mirek ^{[1
]}

Vaculovicova, Marketa ^{[1
]}

机构：

[1] Mendel Univ Brno, Dept Chem & Biochem, Zemedelska 1, Brno 61300, Czech Republic

来源：

MENDELNET 2019: PROCEEDINGS OF 26TH INTERNATIONAL PHD STUDENTS CONFERENCE | 2019年

关键词：

FRET; metallothioneins; oligomerization; capillary electrophoresis; quantum dots; METALLOTHIONEIN;

D O I：

暂无

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Herein, Forster resonance energy transfer (FRET) was used to investigate the oligomerization of mammalian metallothionein (MT) isoform MT-1. A FRET system was developed based on a highly fluorescent ZnCd quantum dot (QD) and cyanine 3 (Cy3) as a powerful tool to probe small distance changes between acceptor and donor fluorophores in nanometer range. In this study, the water-soluble 450-nm emitting ZnCd QDs as donor and 570-nm Cy3 as acceptor were covalently conjugated with MT-1. MetallothioneinMT1 forms dimers (as well as higher oligomers) upon storing under aerobic conditions. These dimers/oligomers were investigated using capillary electrophoresis (CE) coupled with fluorescence detection.

引用

页码：591 / 595

页数：5

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