Data on the role of accessible surface area on osmolytes-induced protein stabilization

This paper describes data related to the research article “Testing the dependence of stabilizing effect of osmolytes on the fractional increase in the accessible surface area on thermal and chemical denaturations of proteins” [1]. Heat- and guanidinium chloride (GdmCl)-induced denaturation of three...

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Autores principales: Rahman, Safikur, Ali, Syed Ausaf, Islam, Asimul, Hassan, Md. Imtaiyaz, Ahmad, Faizan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Data Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5137338/
https://www.ncbi.nlm.nih.gov/pubmed/27942568
http://dx.doi.org/10.1016/j.dib.2016.11.055
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author Rahman, Safikur
Ali, Syed Ausaf
Islam, Asimul
Hassan, Md. Imtaiyaz
Ahmad, Faizan
author_facet Rahman, Safikur
Ali, Syed Ausaf
Islam, Asimul
Hassan, Md. Imtaiyaz
Ahmad, Faizan
author_sort Rahman, Safikur
collection PubMed
description This paper describes data related to the research article “Testing the dependence of stabilizing effect of osmolytes on the fractional increase in the accessible surface area on thermal and chemical denaturations of proteins” [1]. Heat- and guanidinium chloride (GdmCl)-induced denaturation of three disulfide free proteins (bovine cytochrome c (b-cyt-c), myoglobin (Mb) and barstar) in the presence of different concentrations of methylamines (sarcosine, glycine-betaine (GB) and trimethylamine-N-oxide (TMAO)) was monitored by [ϴ](222), the mean residue ellipticity at 222 nm at pH 7.0. Methylamines belong to a class of osmolytes known to protect proteins from deleterious effect of urea. This paper includes comprehensive thermodynamic data obtained from the heat- and GdmCl-induced denaturations of barstar, b-cyt-c and Mb.
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spelling pubmed-51373382016-12-09 Data on the role of accessible surface area on osmolytes-induced protein stabilization Rahman, Safikur Ali, Syed Ausaf Islam, Asimul Hassan, Md. Imtaiyaz Ahmad, Faizan Data Brief Data Article This paper describes data related to the research article “Testing the dependence of stabilizing effect of osmolytes on the fractional increase in the accessible surface area on thermal and chemical denaturations of proteins” [1]. Heat- and guanidinium chloride (GdmCl)-induced denaturation of three disulfide free proteins (bovine cytochrome c (b-cyt-c), myoglobin (Mb) and barstar) in the presence of different concentrations of methylamines (sarcosine, glycine-betaine (GB) and trimethylamine-N-oxide (TMAO)) was monitored by [ϴ](222), the mean residue ellipticity at 222 nm at pH 7.0. Methylamines belong to a class of osmolytes known to protect proteins from deleterious effect of urea. This paper includes comprehensive thermodynamic data obtained from the heat- and GdmCl-induced denaturations of barstar, b-cyt-c and Mb. Elsevier 2016-11-23 /pmc/articles/PMC5137338/ /pubmed/27942568 http://dx.doi.org/10.1016/j.dib.2016.11.055 Text en © 2017 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Rahman, Safikur
Ali, Syed Ausaf
Islam, Asimul
Hassan, Md. Imtaiyaz
Ahmad, Faizan
Data on the role of accessible surface area on osmolytes-induced protein stabilization
title Data on the role of accessible surface area on osmolytes-induced protein stabilization
title_full Data on the role of accessible surface area on osmolytes-induced protein stabilization
title_fullStr Data on the role of accessible surface area on osmolytes-induced protein stabilization
title_full_unstemmed Data on the role of accessible surface area on osmolytes-induced protein stabilization
title_short Data on the role of accessible surface area on osmolytes-induced protein stabilization
title_sort data on the role of accessible surface area on osmolytes-induced protein stabilization
topic Data Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5137338/
https://www.ncbi.nlm.nih.gov/pubmed/27942568
http://dx.doi.org/10.1016/j.dib.2016.11.055
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