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Updated: Aug 24, 2026

Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Published on: May 29, 2011
Effect of binding and conformation on fluorescence quenching in new 2',7'-dichlorofluorescein derivatives
Brian A Sparano1, Shatrughan P Shahi, Kazunori Koide
1Department of Chemistry, University of Pittsburgh, 219 Parkman Avenue, Pittsburgh, Pennsylvania 15260, USA.
Abstract:
[structure: see text] Symmetrical and unsymmetrical 2',7'-dichlorofluorescein (DCF) derivatives have been synthesized by means of Mannich reactions and an aromatic Claisen rearrangement. NMR and fluorescence spectroscopic studies reveal the correlation between the conformations, the photoinduced electron transfer mechanism, and fluorescent intensities of these DCF derivatives. Two quenching nitrogen atoms cooperatively and reversibly suppress the fluorescence of the chromophore.

