Forster resonance energy transfer on single molecules: biological applications

Forster resonance energy transfer on single molecules: biological applications Single molecule observations allow the biologists to obtain mechanistic informations on biological molecules, otherwise inaccessible by classical methods, which rely on the observation of a heterogeneous ensemble of dynamic and unsynchronized molecules. Forster resonance energy transfer (FRET) on single molecules allows the measurement of the distance and distance changes between two fluorophores, in real time. This technique has allowed in the past ten years a better understanding of the mecanochemistry of some molecular motors, such as those implicated for example in DNA replication, translocation or transcription, or protein synthesis (translation). This paper covers the theory and practical aspects of single molecule FRET, and reviews some biological applications.