% IMPORTANT: The following is UTF-8 encoded. This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.
@ARTICLE{Erhan:887724,
author = {Erhan, R. V. and Bodnarchuk, V. and Radulescu, Aurel and
Anghel, L.},
title = {{S}mall {A}ngle {N}eutron {S}cattering {R}eveals {D}imeric
{G}lucose {O}xidase from {A}spergillus niger at p{H} 5.9},
journal = {Journal of surface investigation},
volume = {14},
number = {S1},
issn = {1819-7094},
address = {Berlin},
publisher = {Springer Science+Business Media},
reportid = {FZJ-2020-04381},
pages = {S5 - S10},
year = {2020},
note = {Bitte Post-print ergänzen},
abstract = {Glucose oxidase (GOx) is a 160 kDa flavoenzyme dimer
belonging to the family of glucose-methanol-choline
oxidoreductases. Despite the abundant availability of
information regarding the structure and mechanisms of
interactions of GOx, there is still considerable interest in
studying the properties of this protein to extend its
bio-applications. The present study aims at investigating
the conformational stability of GOx from Aspergillus niger
in the optimal environment that presumably preserves its
functional properties using small angle neutron scattering
method. This method allowed computing the low-resolution
three-dimensional models of the protein. Obtained results
indicate protein dimerization in buffer solution pH 5.9,
with a maximum particle dimension, Dmax, of 110 Å and Rg of
34.50 ± 0.025 Å.},
cin = {JCNS-1 / JCNS-FRM-II / MLZ},
ddc = {540},
cid = {I:(DE-Juel1)JCNS-1-20110106 /
I:(DE-Juel1)JCNS-FRM-II-20110218 / I:(DE-588b)4597118-3},
pnm = {6G4 - Jülich Centre for Neutron Research (JCNS) (POF3-623)
/ 6G15 - FRM II / MLZ (POF3-6G15)},
pid = {G:(DE-HGF)POF3-6G4 / G:(DE-HGF)POF3-6G15},
experiment = {EXP:(DE-MLZ)KWS2-20140101},
typ = {PUB:(DE-HGF)16},
UT = {WOS:000578828100002},
doi = {10.1134/S1027451020070125},
url = {https://juser.fz-juelich.de/record/887724},
}