Pushing the Limits of Luminescence Thermometry: Probing the Temperature
of Proteins in Cells
Abstract
Proteins are involved in numerous cellular activities such as transport
and catalysis. Misfolding during biosynthesis and malfunctioning as a
molecular machine may lead to physiological disorders and metabolic
problems. Protein folding and mechanical work may be viewed as
thermodynamic energetically favorable processes in which stochastic
nonequilibrium intermediate states may be present with conditions such
as thermal fluctuations. In my opinion, measuring those thermal
fluctuations may be a way to access the energy exchange between the
protein and the physiological environment and to better understand how
those nonequilibrium states may influence the misfolding/folding process
and the efficiency of the molecular engine cycle. Here, I discuss
luminescence thermometry as a possible way to measure those temperature
fluctuations from a single molecule experimental perspective with its
current technical limitations and challenges.