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

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

Research output: Chapter or section in a book/report/conference proceeding › Chapter in a published conference proceeding

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.

Original language	English
Title of host publication	Nanophotonics VII
Editors	David L. Andrews, Andreas Ostendorf, Angus J. Bain, Jean-Michel Nunzi
Publisher	SPIE
ISBN (Electronic)	9781510618701
DOIs	https://doi.org/10.1117/12.2306401
Publication status	Published - 4 May 2018
Event	Nanophotonics VII 2018 - Strasbourg, France Duration: 22 Apr 2018 → 26 Apr 2018

Publication series

Name	Proceedings of SPIE - The International Society for Optical Engineering
Volume	10672
ISSN (Print)	0277-786X
ISSN (Electronic)	1996-756X

Conference

Conference	Nanophotonics VII 2018
Country/Territory	France
City	Strasbourg
Period	22/04/18 → 26/04/18

Bibliographical note

Funding Information:
We are grateful to the Engineering & Physical Sciences Research Council for financial support of this work through PhD

Publisher Copyright:
© COPYRIGHT SPIE. Downloading of the abstract is permitted for personal use only.

Keywords

fluorescent protein
FRET
molecular alignment
rotational diffusion
STED
Stimulated Emission Depletion
Two-photon

ASJC Scopus subject areas

Electronic, Optical and Magnetic Materials
Condensed Matter Physics
Computer Science Applications
Applied Mathematics
Electrical and Electronic Engineering

Access to Document

10.1117/12.2306401

Cite this

Masters, T. A., Robinson, N. A., Marsh, R. J., Blacker, T. S., Armoogum, D. A., Larijani, B., & Bain, A. J. (2018). Quadrupole and hexadecapole transition dipole moment alignment in fluorescent protein Homo-FRET. In D. L. Andrews, A. Ostendorf, A. J. Bain, & J.-M. Nunzi (Eds.), Nanophotonics VII Article 106720Y (Proceedings of SPIE - The International Society for Optical Engineering; Vol. 10672). SPIE. https://doi.org/10.1117/12.2306401

Quadrupole and hexadecapole transition dipole moment alignment in fluorescent protein Homo-FRET. / Masters, T. A.; Robinson, N. A.; Marsh, R. J. et al.
Nanophotonics VII. ed. / David L. Andrews; Andreas Ostendorf; Angus J. Bain; Jean-Michel Nunzi. SPIE, 2018. 106720Y (Proceedings of SPIE - The International Society for Optical Engineering; Vol. 10672).

Research output: Chapter or section in a book/report/conference proceeding › Chapter in a published conference proceeding

Masters, TA, Robinson, NA, Marsh, RJ, Blacker, TS, Armoogum, DA, Larijani, B & Bain, AJ 2018, Quadrupole and hexadecapole transition dipole moment alignment in fluorescent protein Homo-FRET. in DL Andrews, A Ostendorf, AJ Bain & J-M Nunzi (eds), Nanophotonics VII., 106720Y, Proceedings of SPIE - The International Society for Optical Engineering, vol. 10672, SPIE, Nanophotonics VII 2018, Strasbourg, France, 22/04/18. https://doi.org/10.1117/12.2306401

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AU - Armoogum, D. A.

AU - Larijani, B.

AU - Bain, A. J.

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N2 - 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.

AB - 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.

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

Abstract

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Bibliographical note

Keywords

ASJC Scopus subject areas

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