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

Safikur Rahman; Syed Ausaf Ali; Asimul Islam; Md Imtaiyaz Hassan; Faizan Ahmad

doi:10.1016/j.dib.2016.11.055

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

Data Brief. 2016 Nov 23:10:47-56. doi: 10.1016/j.dib.2016.11.055. eCollection 2017 Feb.

Authors

Safikur Rahman¹, Syed Ausaf Ali¹, Asimul Islam¹, Md Imtaiyaz Hassan¹, Faizan Ahmad¹

Affiliation

¹ Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi 110025, India.

Abstract

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.

Keywords: Accessible surface area; Gibbs free energy; Methylamines; Osmolytes; Protein stabilization.