Stability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant

Abstract Cytochrome c (cyt c) is widely used as a model protein to study (i) folding and stability aspects of the protein folding problem and (ii) structure–function relationship from the evolutionary point of view. Databases of cyts c now contain 285 cyt c sequences from different organisms. A sequ...

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Autores principales:	Abdullah Naiyer, Bushra Khan, Afzal Hussain, Asimul Islam, Mohamed F. Alajmi, Md. Imtaiyaz Hassan, Monica Sundd, Faizan Ahmad
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0f4c83a6a2004e9290b6a72c653b4c6e
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spelling	oai:doaj.org-article:0f4c83a6a2004e9290b6a72c653b4c6e2021-12-02T16:36:05ZStability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant10.1038/s41598-021-86332-w2045-2322https://doaj.org/article/0f4c83a6a2004e9290b6a72c653b4c6e2021-03-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-86332-whttps://doaj.org/toc/2045-2322Abstract Cytochrome c (cyt c) is widely used as a model protein to study (i) folding and stability aspects of the protein folding problem and (ii) structure–function relationship from the evolutionary point of view. Databases of cyts c now contain 285 cyt c sequences from different organisms. A sequence alignment of all these proteins with respect to horse cyt c led to several important conclusions. One of them is that Leu94 is always conserved in all 30 mammalian cyts c. It is known that mutation L94G of the wild type (WT) horse cyt c is destabilizing and mutant exists as molten globule under the native condition (buffer pH 6 and 25 °C). We have expressed and purified uniformly labeled (13C and 15N) and unlabeled WT horse cyt c and its L94G mutant. We report that labeling does not affect the thermodynamic stability of proteins. To support this conclusion, the secondary and tertiary structure of each protein in labeled and unlabeled forms was determined by conventional techniques (UV–Vis absorption and circular dichroism spectroscopy).Abdullah NaiyerBushra KhanAfzal HussainAsimul IslamMohamed F. AlajmiMd. Imtaiyaz HassanMonica SunddFaizan AhmadNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Abdullah Naiyer Bushra Khan Afzal Hussain Asimul Islam Mohamed F. Alajmi Md. Imtaiyaz Hassan Monica Sundd Faizan Ahmad Stability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant
description	Abstract Cytochrome c (cyt c) is widely used as a model protein to study (i) folding and stability aspects of the protein folding problem and (ii) structure–function relationship from the evolutionary point of view. Databases of cyts c now contain 285 cyt c sequences from different organisms. A sequence alignment of all these proteins with respect to horse cyt c led to several important conclusions. One of them is that Leu94 is always conserved in all 30 mammalian cyts c. It is known that mutation L94G of the wild type (WT) horse cyt c is destabilizing and mutant exists as molten globule under the native condition (buffer pH 6 and 25 °C). We have expressed and purified uniformly labeled (13C and 15N) and unlabeled WT horse cyt c and its L94G mutant. We report that labeling does not affect the thermodynamic stability of proteins. To support this conclusion, the secondary and tertiary structure of each protein in labeled and unlabeled forms was determined by conventional techniques (UV–Vis absorption and circular dichroism spectroscopy).
format	article
author	Abdullah Naiyer Bushra Khan Afzal Hussain Asimul Islam Mohamed F. Alajmi Md. Imtaiyaz Hassan Monica Sundd Faizan Ahmad
author_facet	Abdullah Naiyer Bushra Khan Afzal Hussain Asimul Islam Mohamed F. Alajmi Md. Imtaiyaz Hassan Monica Sundd Faizan Ahmad
author_sort	Abdullah Naiyer
title	Stability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant
title_short	Stability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant
title_full	Stability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant
title_fullStr	Stability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant
title_full_unstemmed	Stability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant
title_sort	stability of uniformly labeled (13c and 15n) cytochrome c and its l94g mutant
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/0f4c83a6a2004e9290b6a72c653b4c6e
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Stability of uniformly labeled (13C and 15N) cytochrome c and its L94G mutant

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