Phototransformable fluorescent proteins (PTFPs) are essential tools for super-resolution (SR) microscopy. Rational engineering of fluorescent proteins exploits the mechanistic information available from structural studies, primarily X-ray crystallography, to design new PTFP variants with improved properties for particular applications. Here we apply solution NMR spectroscopy to study light-induced changes in the conformational dynamics of rsFolder, a reversibly switched fluorescent protein. The dynamic view provided by NMR highlights regions of the protein that comprise mutation points of potential interest for future mutagenesis campaigns.
Collaborations : D. Bourgeois (IBS Grenoble)