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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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

  • 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