English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT

Released

Journal Article

Three photoconvertible forms of Green Fluorescent Protein identified by spectral hole-burning.

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;

External Resource
No external resources are shared
Fulltext (public)

600483.pdf
(Publisher version), 887KB

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. (1999). Three photoconvertible forms of Green Fluorescent Protein identified by spectral hole-burning. Nature Structural and Molecular Biology, 6, 557-560.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0012-FA5C-6
Abstract
Several studies have led to the conclusion that, in the green fluorescent protein (GFP) of the jellyfish Aequorea victoria, a photoconversion involving excited-state proton transfer occurs from an A- to a B-form, while an intermediate I-form was held responsible for the green fluorescence. Here we have identified the I-form of wild-type GFP in absorption, located the 0-0 transitions of all three forms A, B and I, and determined vibrational frequencies of the ground and excited states. The intrinsically narrow 0-0 transitions are revealed by the wavelengths at which holes can be burnt. The pathways of photointerconversion are unraveled by excitation, emission and hole-burning spectroscopy. We present an energy-level scheme that has significant implications for GFP-mutants, which likewise can occur in the three photo-interconvertible forms.