English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Photophysics and optical switching in green fluorescent protein mutants.

MPS-Authors
/persons/resource/persons15895

Subramaniam,  V.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

/persons/resource/persons15286

Jovin,  T. M.
Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society;

Locator
There are no locators available
Fulltext (public)
There are no public fulltexts available
Supplementary Material (public)
There is no public supplementary material available
Citation

Creemers, T. M. H., Lock, A. J., Subramaniam, V., Jovin, T. M., & Voelker, S. (2000). Photophysics and optical switching in green fluorescent protein mutants. Proceedings of the National Academy of Sciences USA, 97, 2974-2978.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-F814-7
Abstract
We demonstrate by using low-temperature high-resolution spectroscopy that red-shifted mutants of green fluorescent protein are photo-interconverted among three conformations and are, therefore, not photostable "one-color" systems as previously believed. From our experiments we have further derived the energy-level schemes governing the interconversion among the three forms. These results have significant implications for the molecular and cell biological applications of the green fluorescent protein family; for example, in fluorescence resonant energy transfer experiments, a change in "color" on irradiation may not necessarily be due to energy transfer but can also arise from a photo-induced conversion between conformers of the excited species.