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

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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Main Authors: Safikur Rahman, Syed Ausaf Ali, Asimul Islam, Md. Imtaiyaz Hassan, Faizan Ahmad
Format: Article
Language:English
Published: Elsevier 2017-02-01
Series:Data in Brief
Subjects:
Osmolytes
Methylamines
Protein stabilization
Accessible surface area
Gibbs free energy
Online Access:http://www.sciencedirect.com/science/article/pii/S2352340916307156
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spelling doaj-0bf812ae3c084fc48009075db34906f52020-11-25T01:34:24ZengElsevierData in Brief2352-34092017-02-0110C475610.1016/j.dib.2016.11.055Data on the role of accessible surface area on osmolytes-induced protein stabilizationSafikur RahmanSyed Ausaf AliAsimul IslamMd. Imtaiyaz HassanFaizan AhmadThis 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.http://www.sciencedirect.com/science/article/pii/S2352340916307156OsmolytesMethylaminesProtein stabilizationAccessible surface areaGibbs free energy
collection DOAJ
language English
format Article
sources DOAJ
author Safikur Rahman
Syed Ausaf Ali
Asimul Islam
Md. Imtaiyaz Hassan
Faizan Ahmad
spellingShingle Safikur Rahman
Syed Ausaf Ali
Asimul Islam
Md. Imtaiyaz Hassan
Faizan Ahmad
Data on the role of accessible surface area on osmolytes-induced protein stabilization
Data in Brief
Osmolytes
Methylamines
Protein stabilization
Accessible surface area
Gibbs free energy
author_facet Safikur Rahman
Syed Ausaf Ali
Asimul Islam
Md. Imtaiyaz Hassan
Faizan Ahmad
author_sort Safikur Rahman
title 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_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_sort data on the role of accessible surface area on osmolytes-induced protein stabilization
publisher Elsevier
series Data in Brief
issn 2352-3409
publishDate 2017-02-01
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.
topic Osmolytes
Methylamines
Protein stabilization
Accessible surface area
Gibbs free energy
url http://www.sciencedirect.com/science/article/pii/S2352340916307156
work_keys_str_mv AT safikurrahman dataontheroleofaccessiblesurfaceareaonosmolytesinducedproteinstabilization
AT syedausafali dataontheroleofaccessiblesurfaceareaonosmolytesinducedproteinstabilization
AT asimulislam dataontheroleofaccessiblesurfaceareaonosmolytesinducedproteinstabilization
AT mdimtaiyazhassan dataontheroleofaccessiblesurfaceareaonosmolytesinducedproteinstabilization
AT faizanahmad dataontheroleofaccessiblesurfaceareaonosmolytesinducedproteinstabilization
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