Multimodal spectroscopy (smFRET, EPR, SAXS, and SANS) and integrative structural modeling reveal large-scale domain rearrangements in human guanylate binding protein 1 (hGBP1) that are driving forces for the formation of oligomers that enable its biological function in innate immune defense.

Single-molecule fluorescence spectroscopy and molecular dynamics simulations illuminate the structure and dynamics of PSD-95, a protein involved in neural plasticity.

Single-molecule force and fluorescence spectroscopy reveal the structural states and dynamics of E. coli single-stranded DNA binding proteins and the energy landscape of the nucleo–protein complex.

Individual SSB-ssDNA complexes undergo reversible condensation and de-condensation that is modulated by RecOR during recombination.

A physics-based, statistically rigorous mathematical model enables automated, objective interpretation of images from single-molecule fluorescence colocalization microscopy experiments.

The conformational dynamics of multidrug resistance protein 1 (MRP1) are tracked in real time by single-molecule fluorescence resonance energy transfer experiments, which elucidate the rate-limiting mechanism of MRP1's transport cycle.

Single molecule experiments reveal competition between spliceosome activation and the discard of the triple small nuclear ribonucleoprotein complex.

Single-molecule observations reveal a mechanism that may be used by multiple competing regulatory proteins to control ribosomal RNA production during rapid bacterial cell growth.

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

Mars provides a software platform for the development of complex single-molecule analysis workflows enabling the discovery and reporting of new biological phenomena with an open data format accessible to everyone.