Abstract
Bimolecular fluorescence complementation is a method of probing protein-ligand interactions under physiological conditions. It provides a state-of-the-art tool to examine interactions observed in 3D structures of multi-component protein complexes, either to validate new experimental structures or to assess the correctness of homology models. Applications of the method range from homo- and hetero-oligomeric assemblies, including non-protein-ligands. Proof-of-principle experiments have also shown the potential of bimolecular fluorescence complementation to monitor protein complexes in a conformation-dependent manner. Here, recent highlights of structure-based applications of the method are outlined and assessed in terms of project-specific findings. These examples demonstrate the power of bimolecular fluorescence complementation to become a leading analysis tool in structural biology, to independently evaluate and characterize higher-order protein complexes.
| Original language | English |
|---|---|
| Journal | Methods |
| Volume | 45 |
| Issue number | 3 |
| Pages (from-to) | 219-222 |
| Number of pages | 4 |
| ISSN | 1046-2023 |
| DOIs | |
| Publication status | Published - 07.2008 |
Funding
We acknowledge the collaboration with Mathias Gautel and Stefan Lange on previous BiFC assays of the titin–telethonin complex. The work has been supported by the European Integrated Project SPINE-2 complexes to M.W. (031220) and by the European Integrated Project 3D Repertoire to M.W. (512028).
