Implementation of FRET Spectrometry Using Temporally Resolved Fluorescence: A Feasibility Study.

Förster resonance energy transfer (FRET) spectrometry is a method for determining the quaternary structure of protein oligomers from distributions of FRET efficiencies that are drawn from pixels of fluorescence images of cells expressing the proteins of interest. FRET spectrometry protocols currently rely on obtaining spectrally resolved fluorescence data from intensity-based experiments. Another imaging method, fluorescence lifetime imaging microscopy (FLIM), is a widely used alternative to compute FRET efficiencies for each pixel in an image from the reduction of the fluorescence lifetime of the donors caused by FRET.

Real time monitoring of the evolution of an epidemic regarded as a physical relaxation process.

The emergence of an epidemic evokes the need to monitor its spread and assess and validate any mitigation measures enacted by governments and administrative bodies in real time. We present here a method based on previous models of relaxation in fractal structures to observe and quantify this spread and the response of affected populations and governing bodies, and apply it to COVID-19 as a case study. This method provides means to simultaneously track in real time quantities such as the mortality and the recovery rates as well as the number of new infections caused by an infected person.