FRET, or fluorescent resonance energy transfer, is an imaging techniques used to visualize interactions between proteins in real time. E-FRET is a more powerful version of FRET which accounts for ...

The coulombic, dipole-dipole interaction needs spectral overlap between an acceptor’s absorption and the donor emission, along with the appropriate orientation of their transition dipoles. This ...

Fluorophore is the specific region or structural domain of a protein that exhibits fluorescence. In any fluorescence spectroscopy, fluorophores are the most significant part to image the ...

Use of helper interactions to encourage weak heteromeric interactions between fluorescent protein pairs helps ensure optimal fluorescence resonance energy transfer (FRET) signals and minimizes the ...