Corseto: A Kinesthetic Garment for Designing, Composing for, and Experiencing an Intersubjective Haptic Voice

We present a novel intercorporeal experience - an intersubjective haptic voice. Through an autobiographical design inquiry, based on singing techniques from the classical opera tradition, we created Corsetto, a kinesthetic garment for transferring somatic reminiscents of vocal experience from an expert singer to a listener. We then composed haptic gestures enacted in the Corsetto, emulating upper-body movements of the live singer performing a piece by Morton Feldman named Three Voices. The gestures in the Corsetto added a haptics-based \u27fourth voice\u27 to the immersive opera performance. Finally, we invited audiences who were asked to wear Corsetto during live performances. Afterwards they engaged in micro-phenomenological interviews. The analysis revealed how the Corsetto managed to bridge inner and outer bodily sensations, creating a feeling of a shared intercorporeal experience, dissolving boundaries between listener, singer and performance. We propose that \u27intersubjective haptics\u27 can be a generative medium not only for singing performances, but other possible intersubjective experiences

Protein-Containing Lipid Bilayers Intercalated with Size-Matched Mesoporous Silica Thin Films

Proteins are key components in a multitude of biological processes, of which the functions carried out by transmembrane (membrane-spanning) proteins are especially demanding for investigations. This is because this class of protein needs to be incorporated into a lipid bilayer representing its native environment, and in addition, many experimental conditions also require a solid support for stabilization and analytical purposes. The solid support substrate may, however, limit the protein functionality due to protein material interactions and a lack of physical space. We have in this work tailored the pore size and pore ordering of a mesoporous silica thin film to match the native cell-membrane arrangement of the transmembrane protein human aquaporin 4 (hAQP4). Using neutron reflectivity (NR), we provide evidence of how substrate pores host the bulky water-soluble domain of hAQP4, which is shown to extend 7.2 nm into the pores of the substrate. Complementary surface analytical tools, including quartz crystal microbalance with dissipation monitoring (QCM-D) and fluorescence microscopy, revealed successful protein-containing supported lipid bilayer (pSLB) formation on mesoporous silica substrates, whereas pSLB formation was hampered on nonporous silica. Additionally, electron microscopy (TEM and SEM), light scattering (DLS and stopped-flow), and small-angle X-ray scattering (SAXS) were employed to provide a comprehensive characterization of this novel hybrid organic-inorganic interface, the tailoring of which is likely to be generally applicable to improve the function and stability of a broad range of membrane proteins containing water-soluble domains