Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
Volume 3, Issue 16, Pages 2298-2302Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jz3008408
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Funding
- UEA
- EPSRC [EP/H02715]
- NSF [CHE-1213047]
- EPSRC [EP/H025715/1] Funding Source: UKRI
- Engineering and Physical Sciences Research Council [EP/H025715/1] Funding Source: researchfish
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1213047] Funding Source: National Science Foundation
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Cis-trans photoisomerization is proposed as a key process in the photoswitching of some photoactivatable fluorescent proteins. Here we present ultrafast fluorescence measurements of the model GFP chromophore (HBDI) in the cis state and in a mixture of the cis and trans states. Our results demonstrate that the mean lifetimes of the cis and trans states are remarkably similar. Therefore, the specific isomer of the chromophore cannot be solely responsible for the different photophysics of the bright and dark states of photoactive proteins, which must therefore be due to differential interactions between the different isomers of the chromophore and the protein.
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