An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states

Crowding effects—important when considering cellular environments—greatly influence protein stability. Here the authors study the impact of macromolecular crowders on high and low temperature protein unfolding, and show that volume exclusion effects are larger when the protein and crowder volumes ar...

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Autores principales:	Caterina Alfano, Domenico Sanfelice, Stephen R. Martin, Annalisa Pastore, Piero Andrea Temussi
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/996b0550a8f049cd81c7f7723f6cdd5f
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spelling	oai:doaj.org-article:996b0550a8f049cd81c7f7723f6cdd5f2021-12-02T14:40:21ZAn optimized strategy to measure protein stability highlights differences between cold and hot unfolded states10.1038/ncomms154282041-1723https://doaj.org/article/996b0550a8f049cd81c7f7723f6cdd5f2017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15428https://doaj.org/toc/2041-1723Crowding effects—important when considering cellular environments—greatly influence protein stability. Here the authors study the impact of macromolecular crowders on high and low temperature protein unfolding, and show that volume exclusion effects are larger when the protein and crowder volumes are similar.Caterina AlfanoDomenico SanfeliceStephen R. MartinAnnalisa PastorePiero Andrea TemussiNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Caterina Alfano Domenico Sanfelice Stephen R. Martin Annalisa Pastore Piero Andrea Temussi An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states
description	Crowding effects—important when considering cellular environments—greatly influence protein stability. Here the authors study the impact of macromolecular crowders on high and low temperature protein unfolding, and show that volume exclusion effects are larger when the protein and crowder volumes are similar.
format	article
author	Caterina Alfano Domenico Sanfelice Stephen R. Martin Annalisa Pastore Piero Andrea Temussi
author_facet	Caterina Alfano Domenico Sanfelice Stephen R. Martin Annalisa Pastore Piero Andrea Temussi
author_sort	Caterina Alfano
title	An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states
title_short	An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states
title_full	An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states
title_fullStr	An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states
title_full_unstemmed	An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states
title_sort	optimized strategy to measure protein stability highlights differences between cold and hot unfolded states
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/996b0550a8f049cd81c7f7723f6cdd5f
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An optimized strategy to measure protein stability highlights differences between cold and hot unfolded states

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