Magnetic control of GFP-like fluorescent proteins - Raw data 2

<p>We've discovered a simple, nontoxic, biocompatible way to control the brightness of&nbsp;<a href="https://www.fpbase.org/protein/avgfp/">GFP</a>-like fluorescent proteins via modest magnetic fields (~10 mT). Fluorescent proteins which seem magnetically inert (e.g.&nbsp;<a href="https://www.fpbase.org/protein/egfp/">EGFP</a>,&nbsp;<a href="https://www.fpbase.org/protein/mscarlet/">mScarlet</a>) become magnetoresponsive in the presence of an appropriate cofactor (e.g. EGFP-<a href="https://doi.org/10.1021/acs.bioconjchem.1c00306">FlavinTag</a>, or an mScarlet/<a href="https://pubchem.ncbi.nlm.nih.gov/compound/Flavin-mononucleotide">FMN</a>&nbsp;solution). This method works at room-temperature and body-temperature,&nbsp;in vitro, in&nbsp;<i>E. coli</i>&nbsp;and in cultured mammalian cells.</p><p>The GFP-family magnetoresponse is weak (ΔF/F≈1%), but shows the hallmarks of evolvability. This suggests exciting technological possibilities, both short-term (e.g. lock-in detection, multiplexing) and long-term (e.g. optically-detected MRI, magnetogenetics).</p><p>We've also discovered weak magnetoresponse from a member of the LOV-domain family. This suggests the possibility that magnetoresponse is a general feature of fluorescent proteins, and not unique to the cryptochrome/photolyase family.</p><p>&nbsp;</p><p>This repository holds some of the raw data for the main text figures. For the contents of the paper, please see: <a href="https://doi.org/10.5281/zenodo.8137174">doi.org/10.5281/zenodo.8137174</a></p>