Data on solubilization, identification, and thermal stability of human Presenilin-2.

ABSTRACT: The data presented here are related to the research article entitled "Expression, purification, and preliminary characterization of human presenilin-2" [1]. Human Presenilin-2 is the catalytic subunit of ?-secretase and a possible calcium leakage channel (Kimberly et al., 2000; Tu et al., 2006) [2], [3]. HisPS2 which was obtained by overexpression in E. coli strain C43 (DE3) was extracted by detergent solubilisation. The sample isolation efficiency by detergents and the protein identification by mass spectrometry and western blot are described. This data article describes the near and far UV circular dichroism measurements and the data deconvolution in terms of secondary structure at 4 and 98?°C. Also, a refolding spectrum is presented. The raw CD spectra used for deconvolution of the helix and stand segments and average length are deposited into Protein Circular Dichroism Data Bank with PCDDBid: CD0005962000 (4?°C far UV), CD0005963000 (98?°C far UV), CD0005964000 (back to 4?°C far UV) and CD0005965000 (4?°C near UV CD).

SUBMITTER: Yang G 

PROVIDER: S-EPMC5852265 | biostudies-literature | 2018 Apr

REPOSITORIES: biostudies-literature