48 research outputs found

    Dynamic inversion of planar-chiral response of terahertz metasurface based on critical transition of checkerboard structures

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    Dynamic inversion of the planar-chiral responses of a metasurface is experimentally demonstrated in the terahertz regime. To realize this inversion, the critical transition of the checkerboard-like metallic structures is used. Resonant structures with planar chirality and their complementary enantiomeric patterns are embedded in the checkerboard. Using vanadium dioxide as a variable resistance, the metasurface is implemented in the terahertz regime. The responses of the metasurface to circularly polarized waves are then characterized by terahertz time-domain spectroscopy. Further, the sign of the circular conversion dichroism, which is closely related to the handedness of the planar chirality of the metasurface, is observed to be inverted at 0.64 THz by varying the temperature. Such invertible planar-chiral responses can be applied practically to the handedness-invertible chiral mirrors

    Phosphorylation-induced conformation of beta(2)-adrenoceptor related to arrestin recruitment revealed by NMR

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    The C-terminal region of G-protein-coupled receptors (GPCRs), stimulated by agonist binding, is phosphorylated by GPCR kinases, and the phosphorylated GPCRs bind to arrestin, leading to the cellular responses. To understand the mechanism underlying the formation of the phosphorylated GPCR-arrestin complex, we performed NMR analyses of the phosphorylated beta(2)-adrenoceptor (beta(2)AR) and the phosphorylated beta(2)AR-beta-arrestin 1 complex, in the lipid bilayers of nanodisc. Here we show that the phosphorylated C-terminal region adheres to either the intracellular side of the transmembrane region or lipids, and that the phosphorylation of the C-terminal region allosterically alters the conformation around M215(5.54) and M279(6.41), located on transemembrane helices 5 and 6, respectively. In addition, we found that the conformation induced by the phosphorylation is similar to that corresponding to the beta-arrestin-bound state. The phosphorylation-induced structures revealed in this study propose a conserved structural motif of GPCRs that enables beta-arrestin to recognize dozens of GPCRs.Peer reviewe
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