A method for rapid high-throughput biophysical analysis of proteins

Abstract Quantitative determination of protein thermodynamic stability is fundamental to many research areas, both basic and applied. Although chemical-induced denaturation is the gold-standard method, it has been replaced in many settings by semi-quantitative approaches such as thermal stability me...

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Autores principales:	Albert Perez-Riba, Laura S. Itzhaki
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/196710379eb84a428f97cdd9d2fb2f5d
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spelling	oai:doaj.org-article:196710379eb84a428f97cdd9d2fb2f5d2021-12-02T16:06:01ZA method for rapid high-throughput biophysical analysis of proteins10.1038/s41598-017-08664-w2045-2322https://doaj.org/article/196710379eb84a428f97cdd9d2fb2f5d2017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08664-whttps://doaj.org/toc/2045-2322Abstract Quantitative determination of protein thermodynamic stability is fundamental to many research areas, both basic and applied. Although chemical-induced denaturation is the gold-standard method, it has been replaced in many settings by semi-quantitative approaches such as thermal stability measurements. The reason for this shift is that chemical denaturation experiments are labour-intensive, sample-costly and time-consuming, and it has been assumed that miniaturisation to a high-throughput format would not be possible without concomitantly comprising data quality. Here we exploit current technologies to create a high-throughput label-free chemical denaturation method that is capable of generating replicate datasets on multiple proteins in parallel on a timescale that is at least ten times faster, much more economical on sample, and with the potential for superior data quality, than the conventional methods used in most research labs currently.Albert Perez-RibaLaura S. ItzhakiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-6 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Albert Perez-Riba Laura S. Itzhaki A method for rapid high-throughput biophysical analysis of proteins
description	Abstract Quantitative determination of protein thermodynamic stability is fundamental to many research areas, both basic and applied. Although chemical-induced denaturation is the gold-standard method, it has been replaced in many settings by semi-quantitative approaches such as thermal stability measurements. The reason for this shift is that chemical denaturation experiments are labour-intensive, sample-costly and time-consuming, and it has been assumed that miniaturisation to a high-throughput format would not be possible without concomitantly comprising data quality. Here we exploit current technologies to create a high-throughput label-free chemical denaturation method that is capable of generating replicate datasets on multiple proteins in parallel on a timescale that is at least ten times faster, much more economical on sample, and with the potential for superior data quality, than the conventional methods used in most research labs currently.
format	article
author	Albert Perez-Riba Laura S. Itzhaki
author_facet	Albert Perez-Riba Laura S. Itzhaki
author_sort	Albert Perez-Riba
title	A method for rapid high-throughput biophysical analysis of proteins
title_short	A method for rapid high-throughput biophysical analysis of proteins
title_full	A method for rapid high-throughput biophysical analysis of proteins
title_fullStr	A method for rapid high-throughput biophysical analysis of proteins
title_full_unstemmed	A method for rapid high-throughput biophysical analysis of proteins
title_sort	method for rapid high-throughput biophysical analysis of proteins
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/196710379eb84a428f97cdd9d2fb2f5d
work_keys_str_mv	AT albertperezriba amethodforrapidhighthroughputbiophysicalanalysisofproteins AT laurasitzhaki amethodforrapidhighthroughputbiophysicalanalysisofproteins AT albertperezriba methodforrapidhighthroughputbiophysicalanalysisofproteins AT laurasitzhaki methodforrapidhighthroughputbiophysicalanalysisofproteins
_version_	1718385132548653056

A method for rapid high-throughput biophysical analysis of proteins

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