A pair of designed transmembrane proteins form a dimer at the cell surface, as seen by single mol... more A pair of designed transmembrane proteins form a dimer at the cell surface, as seen by single molecule imaging. Changes in the linker length or binding domain modulate the 2-dimensional binding affinity.
Opioid receptors (ORs) have been observed as homo- and heterodimers, but it is unclear if the dim... more Opioid receptors (ORs) have been observed as homo- and heterodimers, but it is unclear if the dimers are stable under physiological conditions, and whether monomers or dimers comprise the predominant fraction in a cell. Here, we use three live-cell imaging approaches to assess dimerization of ORs at expression levels that are 10–100 × smaller than in classical biochemical assays. At membrane densities around 25/µm2, a split-GFP assay reveals that κOR dimerizes, while µOR and δOR stay monomeric. At receptor densities
A pair of designed transmembrane proteins form a dimer at the cell surface, as seen by single mol... more A pair of designed transmembrane proteins form a dimer at the cell surface, as seen by single molecule imaging. Changes in the linker length or binding domain modulate the 2-dimensional binding affinity.
Opioid receptors (ORs) have been observed as homo- and heterodimers, but it is unclear if the dim... more Opioid receptors (ORs) have been observed as homo- and heterodimers, but it is unclear if the dimers are stable under physiological conditions, and whether monomers or dimers comprise the predominant fraction in a cell. Here, we use three live-cell imaging approaches to assess dimerization of ORs at expression levels that are 10–100 × smaller than in classical biochemical assays. At membrane densities around 25/µm2, a split-GFP assay reveals that κOR dimerizes, while µOR and δOR stay monomeric. At receptor densities
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Papers by Chenyang Lan