Structural highlights
Function
GFP_AEQVI Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
Publication Abstract from PubMed
Cryoprotection of a protein crystal by addition of small-molecule compounds may sometimes affect the structure of its active site. The spectroscopic and structural effects of the two cryoprotectants glycerol and ethylene glycol on the cyan fluorescent protein Cerulean were investigated. While glycerol had almost no noticeable effect, ethylene glycol was shown to induce a systematic red shift of the UV-vis absorption and fluorescence emission spectra. Additionally, ethylene glycol molecules were shown to enter the core of the protein, with one of them binding in close vicinity to the chromophore, which provides a sound explanation for the observed spectroscopic changes. These results highlight the need to systematically record spectroscopic data on crystals of light-absorbing proteins and reinforce the notion that fluorescent proteins must not been seen as rigid structures.
Alteration of fluorescent protein spectroscopic properties upon cryoprotection.,von Stetten D, Batot GO, Noirclerc-Savoye M, Royant A Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1578-83. doi:, 10.1107/S0907444912037900. Epub 2012 Oct 18. PMID:23090407[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ von Stetten D, Batot GO, Noirclerc-Savoye M, Royant A. Alteration of fluorescent protein spectroscopic properties upon cryoprotection. Acta Crystallogr D Biol Crystallogr. 2012 Nov;68(Pt 11):1578-83. doi:, 10.1107/S0907444912037900. Epub 2012 Oct 18. PMID:23090407 doi:http://dx.doi.org/10.1107/S0907444912037900
