Primary Role of the Chromophore Bond Length Alternation in Reversible Photoconversion of Red Fluorescence Proteins

@inproceedings{Drobizhev2012PrimaryRO,
  title={Primary Role of the Chromophore Bond Length Alternation in Reversible Photoconversion of Red Fluorescence Proteins},
  author={Mikhail Drobizhev and Thomas E Hughes and Yuriy Stepanenko and Pawel Wnuk and K. O'Donnell and J. Nathan Scott and Patrik R. Callis and Alexander G. Mikhaylov and Leslie Dokken and Aleksander Rebane},
  booktitle={Scientific reports},
  year={2012}
}
Rapid photobleaching of fluorescent proteins can limit their use in imaging applications. The underlying kinetics is multi-exponential and strongly depends on the local chromophore environment. The first, reversible, step may be attributed to a rotation around one of the two exocyclic C-C bonds bridging phenol and imidazolinone groups in the chromophore. However it is not clear how the protein environment controls this motion - either by steric hindrances or by modulating the electronic… CONTINUE READING