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Article

Uncovering the hidden ground state of green fluorescent protein.

Proceedings of the National Academy of Sciences of the United States of America - 28 Dec 2004

Kennis John T M, Larsen Delmar S, van Stokkum Ivo H M, Vengris Mikas, van Thor Jasper J, van Grondelle Rienk

Abstract excerpt

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...

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Identifiers

PMID: 15608070
DOI: 10.1073/pnas.0404262102
PMCID: PMC539731

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

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