Monitoring protein activity by resonance energy transfer based on intrinsic fluorescence

Abstract

FRET mechanism was prescribed before few decades. Now, it’s being used mostly in medical science, drug development and pharmaceutical. Its process is dependent on the radiation-free energy conversion between two light responsive chromophores. A donor which is in electronically exited state, passes energy to an acceptor chromophore, by non-radiative dipole-dipole coupling. In FRET, energy is transferred without molecular collision and conversion to thermal energy. The energy conversion leads to a decrease in the fluorescence intensity of the donor and the lifetime of the higher energy level, and an increase in the emission intensity of the acceptor. I would use different references for the assessment of the FRET and through different parameters and frame of references due to surprising results which are based on instrument error and time-based issues.