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  Red-shifted mutants of green fluorescent protein: reversible photoconversions studied by hole-burning and high-resolution spectroscopy

Creemers, T. M. H., Lock, A. J., Subramaniam, V., Jovin, T. M., & Voelker, S. (2002). Red-shifted mutants of green fluorescent protein: reversible photoconversions studied by hole-burning and high-resolution spectroscopy. Chemical Physics, 275(1-3 Sp. Iss. SI), 109-121. Retrieved from http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6TFM-451NBVM-3-3K&_cdi=5230&_user=38661&_pii=S0301010401005377&_origin=search&_coverDate=01%2F01%2F2002&_sk=997249998&view=c&wchp=dGLbVlz-zSkWA&md5=8c5af1380b9ff0c95577dff4723e45c4&ie=/sdarticle.pdf.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-F474-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-E54D-5
Genre: Journal Article

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Creemers, T. M. H.1, Author
Lock, A. J., Author
Subramaniam, V.2, Author              
Jovin, T. M.2, Author              
Voelker, S., Author
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2Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              

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 Abstract: Mutants of green fluorescent protein (GFP) are usually designed to absorb and emit light as "one color" systems, i.e. with a single, photostable conformation of the chromophore. We have studied two red-shifted GFP-mutants (S65T and EYFP) by means of hole-burning and high-resolution optical spectroscopy at low temperature, and compare the data to those previously reported for RS-GFP. We prove that these GFP-mutants are not "one color" systems because they can be reversibly phototransformed from one conformation into another. The results are rationalized in terms of energy-level schemes that are similar to that previously derived by us for wild-type GFP. In these schemes, each mutant can be interconverted by light among at least three conformations that are associated with the protonation-state of the chromophore. The results have relevance for the study of protein-protein interactions by fluorescence resonance energy transfer (FRET), where GFP-mutants of different colors are used as labels in donor-acceptor pairs. Furthermore, we present a detailed mechanism that explains the "on-off" and "blinking" behavior of single GFP-molecules with the proposed energy-level diagrams. (C) 2002 Elsevier Science B.V. All rights reserved.

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Language(s): eng - English
 Dates: 2002-01-01
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Chemical Physics
Source Genre: Journal
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Pages: - Volume / Issue: 275 (1-3 Sp. Iss. SI) Sequence Number: - Start / End Page: 109 - 121 Identifier: -