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@ARTICLE{Yang:844160,
author = {Yang, Ge and Yu, Kun and Kubicek, Jan and Labahn, Jörg},
title = {{D}ata on solubilization, identification, and thermal
stability of human {P}resenilin-2},
journal = {Data in Brief},
volume = {17},
issn = {2352-3409},
address = {Amsterdam [u.a.]},
publisher = {Elsevier},
reportid = {FZJ-2018-01626},
pages = {626 - 630},
year = {2018},
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 γ-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).},
cin = {ICS-6},
ddc = {570},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {551 - Functional Macromolecules and Complexes (POF3-551)},
pid = {G:(DE-HGF)POF3-551},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:29552611},
UT = {WOS:000449763000081},
doi = {10.1016/j.dib.2018.01.039},
url = {https://juser.fz-juelich.de/record/844160},
}