Abstract
The photophysics of the green fluorescent protein is governed by the electronic structure of the chromophore at the heart of its β-barrel protein structure. We present the first two-color, resonance-enhanced, multiphoton ionization spectrum of the isolated neutral chromophore in vacuo with supporting electronic structure calculations. We find the absorption maximum to be 3.65 ± 0.05 eV (340 ± 5 nm), which is blue-shifted by 0.5 eV (55 nm) from the absorption maximum of the protein in its neutral form. Our results show that interactions between the chromophore and the protein have a significant influence on the electronic structure of the neutral chromophore during photoabsorption and provide a benchmark for the rational design of novel chromophores as fluorescent markers or photomanipulators.
Original language | English |
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Pages (from-to) | 3588-3592 |
Journal | Journal of Physical Chemistry Letters |
Volume | 5 |
Early online date | 03 Oct 2014 |
DOIs | |
Publication status | Published - 16 Oct 2014 |
Keywords
- absorption, ultra-violet, time dependent density functional theory, femtosecond, gas-phase
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Dive into the research topics of 'Resonantly Enhanced Multi-Photon Ionization Spectrum of the Neutral Green Fluorescent Protein Chromophore'. Together they form a unique fingerprint.Student theses
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