Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence

We present a new method for high speed tracking of fluorescence time series from single proteins. The method uses a fast sample flow and a modified confocal microscopy, line confocal microscopy, and achieves the time resolution of less than 20 μs. The obtained time series from the B domain of protei...

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Detalles Bibliográficos
Autores principales: Oikawa, Hiroyuki, Suzuki, Yuta, Saito, Masataka, Kamagata, Kiyoto, Arai, Munehito, Takahashi, Satoshi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2013
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3701896/
https://www.ncbi.nlm.nih.gov/pubmed/23827883
http://dx.doi.org/10.1038/srep02151
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author Oikawa, Hiroyuki
Suzuki, Yuta
Saito, Masataka
Kamagata, Kiyoto
Arai, Munehito
Takahashi, Satoshi
author_facet Oikawa, Hiroyuki
Suzuki, Yuta
Saito, Masataka
Kamagata, Kiyoto
Arai, Munehito
Takahashi, Satoshi
author_sort Oikawa, Hiroyuki
collection PubMed
description We present a new method for high speed tracking of fluorescence time series from single proteins. The method uses a fast sample flow and a modified confocal microscopy, line confocal microscopy, and achieves the time resolution of less than 20 μs. The obtained time series from the B domain of protein A labeled with donor and acceptor fluorophores suggest conformational heterogeneity and dynamic fluctuations in the unfolded state.
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spelling pubmed-37018962013-07-05 Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence Oikawa, Hiroyuki Suzuki, Yuta Saito, Masataka Kamagata, Kiyoto Arai, Munehito Takahashi, Satoshi Sci Rep Article We present a new method for high speed tracking of fluorescence time series from single proteins. The method uses a fast sample flow and a modified confocal microscopy, line confocal microscopy, and achieves the time resolution of less than 20 μs. The obtained time series from the B domain of protein A labeled with donor and acceptor fluorophores suggest conformational heterogeneity and dynamic fluctuations in the unfolded state. Nature Publishing Group 2013-07-05 /pmc/articles/PMC3701896/ /pubmed/23827883 http://dx.doi.org/10.1038/srep02151 Text en Copyright © 2013, Macmillan Publishers Limited. All rights reserved http://creativecommons.org/licenses/by-nc-sa/3.0/ This work is licensed under a Creative Commons Attribution-NonCommercial-ShareALike 3.0 Unported License. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-sa/3.0/
spellingShingle Article
Oikawa, Hiroyuki
Suzuki, Yuta
Saito, Masataka
Kamagata, Kiyoto
Arai, Munehito
Takahashi, Satoshi
Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence
title Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence
title_full Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence
title_fullStr Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence
title_full_unstemmed Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence
title_short Microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence
title_sort microsecond dynamics of an unfolded protein by a line confocal tracking of single molecule fluorescence
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3701896/
https://www.ncbi.nlm.nih.gov/pubmed/23827883
http://dx.doi.org/10.1038/srep02151
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