The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy

Solution NMR provides an information-rich technique to monitor the unfolding process and probe the heterogeneity of protein unfolding. Differences in unfolding dynamics of core and peripheral residues during the cold denaturation of Yfh1 are followed in the present study by 1H-15N HSQC spectroscopy.

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Autores principales:	Rita Puglisi, Gogulan Karunanithy, D. Flemming Hansen, Annalisa Pastore, Piero Andrea Temussi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/dbcd8570f9bf4e3c8733224a6a4c24ab
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spelling	oai:doaj.org-article:dbcd8570f9bf4e3c8733224a6a4c24ab2021-12-02T17:20:38ZThe anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy10.1038/s42004-021-00566-32399-3669https://doaj.org/article/dbcd8570f9bf4e3c8733224a6a4c24ab2021-09-01T00:00:00Zhttps://doi.org/10.1038/s42004-021-00566-3https://doaj.org/toc/2399-3669Solution NMR provides an information-rich technique to monitor the unfolding process and probe the heterogeneity of protein unfolding. Differences in unfolding dynamics of core and peripheral residues during the cold denaturation of Yfh1 are followed in the present study by 1H-15N HSQC spectroscopy.Rita PuglisiGogulan KarunanithyD. Flemming HansenAnnalisa PastorePiero Andrea TemussiNature PortfolioarticleChemistryQD1-999ENCommunications Chemistry, Vol 4, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Chemistry QD1-999
spellingShingle	Chemistry QD1-999 Rita Puglisi Gogulan Karunanithy D. Flemming Hansen Annalisa Pastore Piero Andrea Temussi The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
description	Solution NMR provides an information-rich technique to monitor the unfolding process and probe the heterogeneity of protein unfolding. Differences in unfolding dynamics of core and peripheral residues during the cold denaturation of Yfh1 are followed in the present study by 1H-15N HSQC spectroscopy.
format	article
author	Rita Puglisi Gogulan Karunanithy D. Flemming Hansen Annalisa Pastore Piero Andrea Temussi
author_facet	Rita Puglisi Gogulan Karunanithy D. Flemming Hansen Annalisa Pastore Piero Andrea Temussi
author_sort	Rita Puglisi
title	The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
title_short	The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
title_full	The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
title_fullStr	The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
title_full_unstemmed	The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy
title_sort	anatomy of unfolding of yfh1 is revealed by site-specific fold stability analysis measured by 2d nmr spectroscopy
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/dbcd8570f9bf4e3c8733224a6a4c24ab
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The anatomy of unfolding of Yfh1 is revealed by site-specific fold stability analysis measured by 2D NMR spectroscopy

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