An open-source user-friendly toolbox implementing machine learning for single-molecule FRET analysis enabling experts and non-experts to reproducibly provide dynamic structural biology insights.

Development of a real-time SnRK2 kinase FRET reporter reveals rapid SnRK2 activation by ABA, but not by Methyl-Jasmonate or elevated CO2, while directly demonstrating basal SnRK2 activity in guard cells.

Quantitative FRET UPR induction assay is used to measure IRE1 and BIP association and dissociation by a variety of ER misfolded proteins and by an important BiP substrate-binding domain mutant, significantly enhancing the evidence for the allosteric UPR induction model.

VRAC activation, observed with a FRET sensor of intracellular LRRC8-domains movement during gating and by fluorometry, requires plasma membrane localization and diacylglycerol signaling, but is independent of intracellular ionic strength.

The primer extension and 5' flap processing activities of DNA polymerase I are physically coordinated by combined movements of the DNA substrate and the 5' nuclease domain of the enzyme.

A summary of the current “state-of-the-field” of single-molecule FRET used for probing biomolecular structural dynamics.

Fluorescent sensors can track the movement and distribution of the plant hormone abscisic acid in roots and leaves in Arabidopsis.

The combined use of optical trapping and single-molecule FRET permits the study of riboswitch structure formation and conformational dynamics at the same time.

Single molecule FRET reveals that the SWI/SNF-family remodeling enzyme RSC translocates nucleosomes along the DNA in steps of ~1-2 base pairs in size.

Selective import via bacterial ABC importers is facilitated by a hitherto unrecognized complexity in the conformational dynamics of the substrate-binding proteins.