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Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization
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 li...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Crystallographic Association
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6823104/ https://www.ncbi.nlm.nih.gov/pubmed/31700943 http://dx.doi.org/10.1063/1.5120346 |
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author | Auvray, François Dennetiere, David Giuliani, Alexandre Jamme, Frédéric Wien, Frank Nay, Bastien Zirah, Séverine Polack, François Menneglier, Claude Lagarde, Bruno Hirst, Jonathan D. Réfrégiers, Matthieu |
author_facet | Auvray, François Dennetiere, David Giuliani, Alexandre Jamme, Frédéric Wien, Frank Nay, Bastien Zirah, Séverine Polack, François Menneglier, Claude Lagarde, Bruno Hirst, Jonathan D. Réfrégiers, Matthieu |
author_sort | Auvray, François |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6823104 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | American Crystallographic Association |
record_format | MEDLINE/PubMed |
spelling | pubmed-68231042019-11-07 Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization Auvray, François Dennetiere, David Giuliani, Alexandre Jamme, Frédéric Wien, Frank Nay, Bastien Zirah, Séverine Polack, François Menneglier, Claude Lagarde, Bruno Hirst, Jonathan D. Réfrégiers, Matthieu Struct Dyn ARTICLES 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. American Crystallographic Association 2019-10-31 /pmc/articles/PMC6823104/ /pubmed/31700943 http://dx.doi.org/10.1063/1.5120346 Text en © 2019 Author(s). 2329-7778/2019/6(5)/054307/6 All article content, except where otherwise noted, is licensed under a Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | ARTICLES Auvray, François Dennetiere, David Giuliani, Alexandre Jamme, Frédéric Wien, Frank Nay, Bastien Zirah, Séverine Polack, François Menneglier, Claude Lagarde, Bruno Hirst, Jonathan D. Réfrégiers, Matthieu Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization |
title | Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization |
title_full | Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization |
title_fullStr | Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization |
title_full_unstemmed | Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization |
title_short | Time resolved transient circular dichroism spectroscopy using synchrotron natural polarization |
title_sort | time resolved transient circular dichroism spectroscopy using synchrotron natural polarization |
topic | ARTICLES |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6823104/ https://www.ncbi.nlm.nih.gov/pubmed/31700943 http://dx.doi.org/10.1063/1.5120346 |
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