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 …

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 …

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 …

Single-molecule spectroscopy is a powerful method for studying the physics of molecular
systems, particularly biomolecules, such as proteins and nucleic acids. By avoiding …

Optical investigations of nanometer distances between proteins, their subunits, or other
biomolecules have been the exclusive prerogative of Förster resonance energy transfer …

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 …