Quadrupole and hexadecapole transition dipole moment alignment in fluorescent protein Homo-FRET

T. A. Masters; N. A. Robinson; R. J. Marsh; T. S. Blacker; D. A. Armoogum; B. Larijani; A. J. Bain

doi:10.1117/12.2306401

4 May 2018 Quadrupole and hexadecapole transition dipole moment alignment in fluorescent protein Homo-FRET

T. A. Masters, N. A. Robinson, R. J. Marsh, T. S. Blacker, D. A. Armoogum, B. Larijani, A. J. Bain

Proceedings Volume 10672, Nanophotonics VII; 106720Y (2018) https://doi.org/10.1117/12.2306401
Event: SPIE Photonics Europe, 2018, Strasbourg, France

Abstract

Polarized time resolved fluorescence measurements are used to characterise the structure of the two-photon tensor in the enhanced green fluorescent protein (EGFP) and predict the “hidden” degree of hexadecapole transition dipole alignment 〈α₄₀〉 created by two-photon absorption (TPA). We employ a new method for the accurate STED measurement of the evolution of 〈α₄₀〉 by analysing the saturation dynamics of the orthogonally polarized components of two-photon excited EGFP fluorescence as a function of the time delay between the 800 nm pump and 570 nm dump pulses. The relaxation of 〈α₄₀〉 by homo-FRET is found to be considerably greater than that for the fluorescence anisotropy which directly measures the quadrupolar transition dipole moment alignment 〈α₂₀〉. Our results indicate that higher order dipole moment correlation measurements promise to be a sensitive probe of resonance energy transfer dynamics.

Conference Presentation

Citation Download Citation

T. A. Masters, N. A. Robinson, R. J. Marsh, T. S. Blacker, D. A. Armoogum, B. Larijani, and A. J. Bain "Quadrupole and hexadecapole transition dipole moment alignment in fluorescent protein Homo-FRET", Proc. SPIE 10672, Nanophotonics VII, 106720Y (4 May 2018); https://doi.org/10.1117/12.2306401

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