% 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{Rudani:1026937,
author = {Rudani, Binny and Jakubowski, Andre and Kriegs, Hartmut and
Wiegand, Simone},
title = {{D}eciphering the guanidinium cation: {I}nsights into
thermal diffusion},
journal = {The journal of chemical physics},
volume = {160},
number = {21},
issn = {0021-9606},
address = {Melville, NY},
publisher = {American Institute of Physics},
reportid = {FZJ-2024-03529},
pages = {214502},
year = {2024},
abstract = {Thermophoresis, or thermodiffusion, is becoming a more
popular method for investigating the interactions between
proteins and ligands due to its high sensitivity to the
interactions between solutes and water. Despite its growing
use, the intricate mechanisms behind thermodiffusion remain
unclear. This gap in knowledge stems from the complexities
of thermodiffusion in solvents that have specific
interactions, as well as the intricate nature of systems
that include many components with both non-ionic and ionic
groups. ${\color{red}To$ deepen our understanding, we reduce
complexity by conducting systematic studies on aqueous salt
solutions.} In this work, we focused on how guanidinium salt
solutions behave in a temperature gradient, using thermal
diffusion forced Rayleigh scattering experiments at
temperatures ranging from 15 to 35°C. We looked at the
thermodiffusive behavior of four guanidinium salts
(thiocyanate, iodide, chloride, and carbonate) in solutions
with concentrations from 1 to 3 mol/kg. The guanidinium
cation is disk-shaped and is characterized by flat
hydrophobic surfaces and three amine groups, which enable
directional hydrogen bonding along the edges. We compare our
results with the behavior of salts with spherical cations
such as sodium, potassium and lithium. Our discussions are
framed around how different salts are solvated, specifically
in the context of the Hofmeister series, which ranks ions
based on their effects on the solvation of proteins.},
cin = {IBI-4},
ddc = {530},
cid = {I:(DE-Juel1)IBI-4-20200312},
pnm = {5241 - Molecular Information Processing in Cellular Systems
(POF4-524)},
pid = {G:(DE-HGF)POF4-5241},
typ = {PUB:(DE-HGF)16},
pubmed = {38828819},
UT = {WOS:001239198500004},
doi = {10.1063/5.0215843},
url = {https://juser.fz-juelich.de/record/1026937},
}