1. Could you explain the significance of your article to the non-specialist?

There are myriads of papers in which the Förster theory of energy transfer is used for distance measurements in biomacromolecules. Actually the Förster theory is very crude for most of these applications, since it does not account for the influence of local motions and reorientations of the interacting fluorescent molecules. In the present work an extended Förster theory (EFT) is applied for the first time in the analyses of data. The paper demonstrates a method for how to use the EFT for determining intramolecular distances in a protein.

2. What has motivated you to conduct this work?

Mainly to develop the electronic energy transfer/migration experiments as more precise tool for obtaining structural information about biomacromolecules. This can complement the established NMR spectroscopy and X-ray diffraction methods.

3. Where do you see this work developing in the future?

For biomacromolecular systems in general, but in particular in the study of proteins, e.g. the structural changes of proteins associated with their interaction with various target molecules.

4. Are there any particular challenges facing future research in this area?

By applying the EFT a fundamental theoretical limitation has been eliminated. The future challenges are likely to use more efficient strategies for achieving faster analyses of the data, as well as to further improve the experimental acquisition of the data.