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Green and Red Fluorescent Proteins: Photo‐ and Thermally Induced Dynamics Probed by Site‐Selective Spectroscopy and Hole Burning
Author(s) -
Bonsma S.,
Purchase R.,
Jezowski S.,
Gallus J.,
Könz F.,
Völker S.
Publication year - 2005
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.200500005
Subject(s) - förster resonance energy transfer , fluorescence , green fluorescent protein , biophysics , chemistry , protein dynamics , spectroscopy , fluorescent protein , photochemistry , protein structure , biology , biochemistry , physics , optics , gene , quantum mechanics
The cloning and expression of autofluorescent proteins in living matter, combined with modern imaging techniques, have thoroughly changed the world of bioscience. In particular, such proteins are widely used as genetically encoded labels to track the movement of proteins as reporters of cellular signals and to study protein–protein interactions by fluorescence resonance energy transfer (FRET). Their optical properties, however, are complex and it is important to understand these for the correct interpretation of imaging data and for the design of new fluorescent mutants. In this Minireview we start with a short survey of the field and then focus on the photo‐ and thermally induced dynamics of green and red fluorescent proteins. In particular, we show how fluorescence line narrowing and high‐resolution spectral hole burning at low temperatures can be used to unravel the photophysics and photochemistry and shed light on the intricate electronic structure of these proteins.