Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization

François Auvray; David Dennetiere; Alexandre Giuliani; Frédéric Jamme; Frank Wien; Bastien Nay; Séverine Zirah; François Polack; Claude Menneglier; Bruno Lagarde; Jonathan D. Hirst; Matthieu Réfrégiers

doi:10.1063/1.5120346

Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization

François Auvray, David Dennetiere, Alexandre Giuliani, Frédéric Jamme, Frank Wien, Bastien Nay, Séverine Zirah, François Polack, Claude Menneglier, Bruno Lagarde, Jonathan D. Hirst, Matthieu Réfrégiers

Research output: Contribution to journal › Article › peer-review

Abstract

Ultraviolet (UV) synchrotron radiation circular dichroism (SRCD) spectroscopy has made an important contribution to the determination and understanding of the structure of bio-molecules. In this paper, we report an innovative approach that we term time-resolved SRCD (tr-SRCD), which overcomes the limitations of current broadband UV SRCD setups. This technique allows accessing ultrafast time scales (down to nanoseconds), previously measurable only by other methods, such as infrared (IR), nuclear magnetic resonance (NMR), fluorescence and absorbance spectroscopies, and small angle X-ray scattering (SAXS). The tr-SRCD setup takes advantage of the natural polarization of the synchrotron radiation emitted by a bending magnet to record broadband UV CD faster than any current SRCD setup, improving the acquisition speed from 10 mHz to 130 Hz and the accessible temporal resolution by several orders of magnitude. We illustrate the new approach by following the isomer concentration changes of an azopeptide after a photoisomerization. This breakthrough in SRCD spectroscopy opens up a wide range of potential applications to the detailed characterization of biological processes, such as protein folding and protein-ligand binding.

Original language	English
Article number	054307
Journal	Structural Dynamics
Volume	6
Issue number	5
DOIs	https://doi.org/10.1063/1.5120346
Publication status	Published - 1 Sept 2019
Externally published	Yes

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title = "Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization",

abstract = "Ultraviolet (UV) synchrotron radiation circular dichroism (SRCD) spectroscopy has made an important contribution to the determination and understanding of the structure of bio-molecules. In this paper, we report an innovative approach that we term time-resolved SRCD (tr-SRCD), which overcomes the limitations of current broadband UV SRCD setups. This technique allows accessing ultrafast time scales (down to nanoseconds), previously measurable only by other methods, such as infrared (IR), nuclear magnetic resonance (NMR), fluorescence and absorbance spectroscopies, and small angle X-ray scattering (SAXS). The tr-SRCD setup takes advantage of the natural polarization of the synchrotron radiation emitted by a bending magnet to record broadband UV CD faster than any current SRCD setup, improving the acquisition speed from 10 mHz to 130 Hz and the accessible temporal resolution by several orders of magnitude. We illustrate the new approach by following the isomer concentration changes of an azopeptide after a photoisomerization. This breakthrough in SRCD spectroscopy opens up a wide range of potential applications to the detailed characterization of biological processes, such as protein folding and protein-ligand binding.",

author = "Fran{\c c}ois Auvray and David Dennetiere and Alexandre Giuliani and Fr{\'e}d{\'e}ric Jamme and Frank Wien and Bastien Nay and S{\'e}verine Zirah and Fran{\c c}ois Polack and Claude Menneglier and Bruno Lagarde and Hirst, \{Jonathan D.\} and Matthieu R{\'e}fr{\'e}giers",

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year = "2019",

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doi = "10.1063/1.5120346",

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T1 - Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization

AU - Auvray, François

AU - Dennetiere, David

AU - Giuliani, Alexandre

AU - Jamme, Frédéric

AU - Wien, Frank

AU - Nay, Bastien

AU - Zirah, Séverine

AU - Polack, François

AU - Menneglier, Claude

AU - Lagarde, Bruno

AU - Hirst, Jonathan D.

AU - Réfrégiers, Matthieu

PY - 2019/9/1

Y1 - 2019/9/1

N2 - Ultraviolet (UV) synchrotron radiation circular dichroism (SRCD) spectroscopy has made an important contribution to the determination and understanding of the structure of bio-molecules. In this paper, we report an innovative approach that we term time-resolved SRCD (tr-SRCD), which overcomes the limitations of current broadband UV SRCD setups. This technique allows accessing ultrafast time scales (down to nanoseconds), previously measurable only by other methods, such as infrared (IR), nuclear magnetic resonance (NMR), fluorescence and absorbance spectroscopies, and small angle X-ray scattering (SAXS). The tr-SRCD setup takes advantage of the natural polarization of the synchrotron radiation emitted by a bending magnet to record broadband UV CD faster than any current SRCD setup, improving the acquisition speed from 10 mHz to 130 Hz and the accessible temporal resolution by several orders of magnitude. We illustrate the new approach by following the isomer concentration changes of an azopeptide after a photoisomerization. This breakthrough in SRCD spectroscopy opens up a wide range of potential applications to the detailed characterization of biological processes, such as protein folding and protein-ligand binding.

AB - Ultraviolet (UV) synchrotron radiation circular dichroism (SRCD) spectroscopy has made an important contribution to the determination and understanding of the structure of bio-molecules. In this paper, we report an innovative approach that we term time-resolved SRCD (tr-SRCD), which overcomes the limitations of current broadband UV SRCD setups. This technique allows accessing ultrafast time scales (down to nanoseconds), previously measurable only by other methods, such as infrared (IR), nuclear magnetic resonance (NMR), fluorescence and absorbance spectroscopies, and small angle X-ray scattering (SAXS). The tr-SRCD setup takes advantage of the natural polarization of the synchrotron radiation emitted by a bending magnet to record broadband UV CD faster than any current SRCD setup, improving the acquisition speed from 10 mHz to 130 Hz and the accessible temporal resolution by several orders of magnitude. We illustrate the new approach by following the isomer concentration changes of an azopeptide after a photoisomerization. This breakthrough in SRCD spectroscopy opens up a wide range of potential applications to the detailed characterization of biological processes, such as protein folding and protein-ligand binding.

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DO - 10.1063/1.5120346

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SN - 2329-7778

VL - 6

JO - Structural Dynamics

JF - Structural Dynamics

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ER -

Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization

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