Uncovering the hidden ground state of green fluorescent protein

J.T.M. Kennis, D.S. Larsen, I.H.M. van Stokkum, M. Vengris, J.J. van Thor, R. van Grondelle

Research output: Contribution to JournalArticleAcademicpeer-review

Abstract

The fluorescence properties of GFP are strongly influenced by the protonation states of its chromophore and nearby amino acid side chains. In the ground state, the GFP chromophore is neutral and absorbs in the near UV. Upon excitation, the chromophore is deprotonated, and the resulting anionic chromophore emits its green fluorescence. So far, only excited-state intermediates have been observed in the GFP photocycle. We have used ultrafast multipulse control spectroscopy to prepare and directly observe GFP's hidden anionic ground-state intermediates as an integral part of the photocycle. Combined with dispersed multichannel detection and advanced global analysis techniques, the existence of two distinct anionic ground-state intermediates, I
Original languageEnglish
Pages (from-to)17988-17993
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume101
Issue number52
DOIs
Publication statusPublished - 28 Dec 2004

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