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Stoner-Ma, Deborah, Jaye, Andrew A., Ronayne, Kate L., Nappa, Jerome, Tonge, Peter J. and Meech, Stephen R. 
ORCID: https://orcid.org/0000-0001-5561-2782
(2008)
Ultrafast electronic and vibrational dynamics of stabilized A state mutants of the green fluorescent protein (GFP): Snipping the proton wire.
Chemical Physics, 350 (1-3).
pp. 193-200.
Abstract
Two blue absorbing and emitting mutants (S65G/T203V/E222Q and S65T at pH 5.5) of the green fluorescent protein (GFP) have been investigated through ultrafast time resolved infra-red (TRIR) and fluorescence spectroscopy. In these mutants, in which the excited state proton transfer reaction observed in wild-type GFP has been blocked, the photophysics are dominated by the neutral A state. It was found that the A* excited state lifetime is short, indicating that it is relatively less stabilised in the protein matrix than the anionic form. However, the lifetime of the A state can be increased through modifications to the protein structure. The TRIR spectra show that a large shifts in protein vibrational modes on excitation of the A state occurs in both these GFP mutants. This is ascribed to a change in H-bonding interactions between the protein matrix and the excited state.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Chemistry |
| UEA Research Groups: | Faculty of Science > Research Groups > Physical and Analytical Chemistry (former - to 2017) Faculty of Science > Research Groups > Chemistry of Light and Energy Faculty of Science > Research Groups > Centre for Photonics and Quantum Science |
| Depositing User: | Rachel Smith |
| Date Deposited: | 23 Mar 2011 13:16 |
| Last Modified: | 09 Feb 2023 13:35 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/27002 |
| DOI: | 10.1016/j.chemphys.2008.02.021 |
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