Förster Resonance Energy Transfer (FRET) for Proteins

Abstract Förster Resonance Energy Transfer (FRET) is a spectroscopic technique applied throughout physics, chemistry, and biology to measure quantitatively the distance between selected locations on macromolecules and to determine the close association between interacting molecular components. Because FRET typically occurs over distances from 0.5 to 10 nm, it is especially useful for investigating many interesting biological molecular structures. It is also particularly valuable for following the dynamics and structural fluctuations of biological molecular systems. FRET can be applied in solution or under imaging conditions (such as in fluorescence microscopy, nanoscience, and even macroscopic imaging). In this article, we discuss the fundamentals of FRET. These principles apply to every FRET measurement. We present the basic rudiments and the relevant literature of FRET to provide the reader with the necessary background essential for understanding much of the past and modern literature. At the end of the article, we give a short discussion of several applications of FRET to proteins. The literature for FRET is vast, and many new applications are constantly being developed. We could not do justice to the many practitioners of FRET in such a short space, but armed with the background that is presented, we hope this basic information will help readers follow much of the literature and apply it in their own work.