4.7 Article

Bimolecular fluorescence complementation in structural biology

Journal

METHODS
Volume 45, Issue 3, Pages 219-222

Publisher

ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.ymeth.2008.06.015

Keywords

bimolecular fluorescence complementation; structural biology; protein complexes; muscle filament assembly; viral capsid assembly; homology model; yellow fluorescent protein

Funding

  1. European Integrated Project SPINE-2 complexes [031220]
  2. European Integrated Project 3D Repertoire [512028]

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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. (C) 2008 Elsevier Inc. All rights reserved.

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