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...

Full description

Saved in:

Bibliographic Details
Main Authors:	Caterina Alfano, Domenico Sanfelice, Stephen R. Martin, Annalisa Pastore, Piero Andrea Temussi
Format:	article
Language:	EN
Published:	Nature Portfolio 2017
Subjects:	Science Q
Online Access:	https://doaj.org/article/996b0550a8f049cd81c7f7723f6cdd5f
Tags:	Add Tag No Tags, Be the first to tag this record!

id	oai:doaj.org-article:996b0550a8f049cd81c7f7723f6cdd5f
record_format	dspace
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
work_keys_str_mv	AT caterinaalfano anoptimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT domenicosanfelice anoptimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT stephenrmartin anoptimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT annalisapastore anoptimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT pieroandreatemussi anoptimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT caterinaalfano optimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT domenicosanfelice optimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT stephenrmartin optimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT annalisapastore optimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates AT pieroandreatemussi optimizedstrategytomeasureproteinstabilityhighlightsdifferencesbetweencoldandhotunfoldedstates
_version_	1718390312642019328

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

Similar Items