Ultrafast electronic and vibrational dynamics of stabilized A state mutants of the green fluorescent protein (GFP): Snipping the proton wire

Stoner-Ma, Deborah, Jaye, Andrew A., Ronayne, Kate L., Nappa, Jerome, Tonge, Peter J. and Meech, Stephen R. (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.

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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
Depositing User: Rachel Smith
Date Deposited: 23 Mar 2011 13:16
Last Modified: 04 Oct 2019 15:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/27002
DOI: 10.1016/j.chemphys.2008.02.021

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