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@ARTICLE{Sarter:1007490,
author = {Sarter, Mona and Niether, Doreen and Wiegand, Simone and
Fitter, Joerg and Stadler, Andreas M.},
title = {{C}omplementary approaches to obtaining thermodynamic
parameters from protein ligand systems-challenges and
opportunities},
journal = {The European physical journal / Web of Conferences},
volume = {272},
issn = {2100-014X},
address = {Les Ulis},
publisher = {EDP Sciences},
reportid = {FZJ-2023-02080},
pages = {01016 -},
year = {2022},
abstract = {Protein ligand interactions play an important role in
biology. Increasingly the aim is to understandand influence
protein ligand binding. The binding process is heavily
influenced by its thermodynamicparameters. In order to
understand how the whole system thermodynamics work it is
important to characterisethe individual contribution of each
of the systems components. While the change in
conformational entropyof the protein can be determined using
QENS complementary methods are necessary in order to
characteriseall components. This paper will describe the
challenges that can occur when combining the different
methods,as well as how they can be overcome.},
cin = {IBI-6 / ER-C-3 / JCNS-1 / IBI-8 / IBI-4},
ddc = {530},
cid = {I:(DE-Juel1)IBI-6-20200312 / I:(DE-Juel1)ER-C-3-20170113 /
I:(DE-Juel1)JCNS-1-20110106 / I:(DE-Juel1)IBI-8-20200312 /
I:(DE-Juel1)IBI-4-20200312},
pnm = {5352 - Understanding the Functionality of Soft Matter and
Biomolecular Systems (POF4-535) / 5241 - Molecular
Information Processing in Cellular Systems (POF4-524)},
pid = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
typ = {PUB:(DE-HGF)16},
doi = {10.1051/epjconf/202227201016},
url = {https://juser.fz-juelich.de/record/1007490},
}