Protein Stability in TMAO and Mixed Urea-TMAO Solutions
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F20%3A43920571" target="_blank" >RIV/60461373:22340/20:43920571 - isvavai.cz</a>
Result on the web
<a href="https://pubs.acs.org/doi/10.1021/acs.jpcb.0c04357" target="_blank" >https://pubs.acs.org/doi/10.1021/acs.jpcb.0c04357</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.jpcb.0c04357" target="_blank" >10.1021/acs.jpcb.0c04357</a>
Alternative languages
Result language
angličtina
Original language name
Protein Stability in TMAO and Mixed Urea-TMAO Solutions
Original language description
Osmolytes are essential for cellular function under ubiquitous osmotic stress. Trimethylamine N-oxide (TMAO) is one such osmolyte that has gained remarkable attention due to its protein-protective ability against urea. This Review aims at providing a detailed account of recent theoretical and experimental developments in characterizing the structural changes and thermodynamic stability of proteins in the presence of TMAO and urea. New vapor pressure osmometry and molecular dynamics simulation results on urea–TMAO solutions are presented, and a unified molecular mechanism of TMAO counteraction of urea-induced protein denaturation is introduced. In addition, a detailed technical assessment of molecular dynamics force fields for TMAO and for urea–TMAO solutions is presented. The force field analysis highlights how many of the commonly used force field models are in fact incompatible with solvation thermodynamics and can lead to misleading conclusions. A new optimized force field for TMAO (Shea(m)) is presented, and a recently optimized force field for TMAO–urea (Netz(m)) that best reproduces experimental data is highlighted.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/GA20-24155S" target="_blank" >GA20-24155S: Insight in preferential interactions, bridging, and cononsolvency on PNIPAM by experimental and computational thermodynamics</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Physical Chemistry B
ISSN
1520-6106
e-ISSN
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Volume of the periodical
124
Issue of the periodical within the volume
29
Country of publishing house
US - UNITED STATES
Number of pages
17
Pages from-to
"6181–6197"
UT code for WoS article
000555505200001
EID of the result in the Scopus database
2-s2.0-85088607484