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A disordered tether to iLID improves photoswitchable protein patterning on model membranes.
Daniele Di Iorio, Johanna Bergmann, Sayuri L Higashi, Arne Hoffmann, Seraphine V Wegner
Chemical communications (Cambridge, England) 2023 Apr 06Sizes of these terms reflect their relevance to your search.
Reversible protein patterning on model membranes is important to reproduce spatiotemporal protein dynamics in vitro. An engineered version of iLID, disiLID, with a disordered domain as a membrane tether improves the recruitment of Nano under blue light and the reversibility in the dark, which enables protein patterning on membranes with higher spatiotemporal precision.
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Daniele Di Iorio, Johanna Bergmann, Sayuri L Higashi, Arne Hoffmann, Seraphine V Wegner. A disordered tether to iLID improves photoswitchable protein patterning on model membranes. Chemical communications (Cambridge, England). 2023 Apr 06;59(29):4380-4383
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PMID: 36946614
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