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A disordered tether to iLID improves photoswitchable protein patterning on model membranes.

Daniele Di IorioJohanna BergmannSayuri L HigashiArne HoffmannSeraphine Valeska Wegner
Published in: Chemical communications (Cambridge, England) (2023)
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.
Keyphrases
  • protein protein
  • amino acid
  • binding protein
  • psychometric properties