Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering

Femtosecond time-resolved X-ray solution scattering (fs-TRXSS) measurements provide information on the structural dynamics of proteins in solution. Here, the authors present a structure refinement method for the analysis of fs-TRXSS data and use it to characterise the ultrafast structural changes of...

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Autores principales: Yunbeom Lee, Jong Goo Kim, Sang Jin Lee, Srinivasan Muniyappan, Tae Wu Kim, Hosung Ki, Hanui Kim, Junbeom Jo, So Ri Yun, Hyosub Lee, Kyung Won Lee, Seong Ok Kim, Marco Cammarata, Hyotcherl Ihee
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Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/544dee08ed074971a9fa1c55d740e043
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spelling oai:doaj.org-article:544dee08ed074971a9fa1c55d740e0432021-12-02T16:04:16ZUltrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering10.1038/s41467-021-23947-72041-1723https://doaj.org/article/544dee08ed074971a9fa1c55d740e0432021-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-23947-7https://doaj.org/toc/2041-1723Femtosecond time-resolved X-ray solution scattering (fs-TRXSS) measurements provide information on the structural dynamics of proteins in solution. Here, the authors present a structure refinement method for the analysis of fs-TRXSS data and use it to characterise the ultrafast structural changes of homodimeric haemoglobin.Yunbeom LeeJong Goo KimSang Jin LeeSrinivasan MuniyappanTae Wu KimHosung KiHanui KimJunbeom JoSo Ri YunHyosub LeeKyung Won LeeSeong Ok KimMarco CammarataHyotcherl IheeNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Yunbeom Lee
Jong Goo Kim
Sang Jin Lee
Srinivasan Muniyappan
Tae Wu Kim
Hosung Ki
Hanui Kim
Junbeom Jo
So Ri Yun
Hyosub Lee
Kyung Won Lee
Seong Ok Kim
Marco Cammarata
Hyotcherl Ihee
Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering
description Femtosecond time-resolved X-ray solution scattering (fs-TRXSS) measurements provide information on the structural dynamics of proteins in solution. Here, the authors present a structure refinement method for the analysis of fs-TRXSS data and use it to characterise the ultrafast structural changes of homodimeric haemoglobin.
format article
author Yunbeom Lee
Jong Goo Kim
Sang Jin Lee
Srinivasan Muniyappan
Tae Wu Kim
Hosung Ki
Hanui Kim
Junbeom Jo
So Ri Yun
Hyosub Lee
Kyung Won Lee
Seong Ok Kim
Marco Cammarata
Hyotcherl Ihee
author_facet Yunbeom Lee
Jong Goo Kim
Sang Jin Lee
Srinivasan Muniyappan
Tae Wu Kim
Hosung Ki
Hanui Kim
Junbeom Jo
So Ri Yun
Hyosub Lee
Kyung Won Lee
Seong Ok Kim
Marco Cammarata
Hyotcherl Ihee
author_sort Yunbeom Lee
title Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering
title_short Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering
title_full Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering
title_fullStr Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering
title_full_unstemmed Ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond X-ray solution scattering
title_sort ultrafast coherent motion and helix rearrangement of homodimeric hemoglobin visualized with femtosecond x-ray solution scattering
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/544dee08ed074971a9fa1c55d740e043
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