Fluorescence resonance energy transfer (FRET) is a powerful spectroscopic method for
measuring distances in the 2–8 nm range. Often, conformational changes and molecular …

Chemists can now use molecules to mimic the concepts and equipment of mathematics and
computer science. Recently, there has been growth in the integration of logic gates onto tiny …

Biomolecular condensates formed via phase separation of proteins and nucleic acids are
thought to be associated with a wide range of cellular functions and dysfunctions. We dissect …

Single-molecule FRET (smFRET) is a versatile technique to study the dynamics and function
of biomolecules since it makes nanoscale movements detectable as fluorescence signals …

Many proteins require different structural states or conformations for function, and
intrinsically disordered proteins, ie proteins without stable three-dimensional structure, are …

Single-molecule experiments have changed the way we explore the physical world, yet data
analysis remains time-consuming and prone to human bias. Here, we introduce Deep-LASI …

Over the past decades, single-molecule and super-resolution microscopy have advanced
and represent essential tools for life science research. There is, however, a growing gap …

Unraveling the concentration-dependent spatiotemporal organization of receptors in the
plasma membrane is crucial to understand cell signal initiation. A paradigm of this process is …

Understanding the fluorescence resonance energy transfer (FRET) of metal nanoparticles at
the atomic level has long been a challenge due to the lack of accurate systems with definite …

Single-molecule FRET (smFRET) has become a versatile tool for probing the structure and
functional dynamics of biomolecular systems, and is extensively used to address questions …