Cation-π Interactions in Biomolecular Contexts by Neutron Scattering and Molecular Dynamics: A Case Study of the Tetramethylammonium Cation

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00637276" target="_blank" >RIV/61388963:_____/25:00637276 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1021/acs.jpcb.5c02001" target="_blank" >https://doi.org/10.1021/acs.jpcb.5c02001</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.jpcb.5c02001" target="_blank" >10.1021/acs.jpcb.5c02001</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Cation-π Interactions in Biomolecular Contexts by Neutron Scattering and Molecular Dynamics: A Case Study of the Tetramethylammonium Cation

Popis výsledku v původním jazyce

Cation−π interactions involving the tetramethylammonium motif are prevalent in biological systems, playing crucial roles in membrane protein function, DNA expression regulation, and protein folding. However, accurately modeling cation−π interactions where electronic polarization plays a critical role is computationally challenging, especially in large biomolecular systems. This study implements a physically justified electronic continuum correction (ECC) to the CHARMM36 force field, scaling ionic charges by a factor of 0.75 to effectively account for electronic polarization without additional computational overhead. This approach, while not specifically designed for cation−π interactions, is shown here to significantly improve predictions of the structure of an aqueous tetramethylammonium–pyridine complex as compared to neutron diffraction data. This result, together with computational predictions for the structure of the aqueous tetramethylammonium–phenol complex, underscores the potential of ECC as a versatile method to improve the description of cation−π interactions in biomolecular simulations.

Název v anglickém jazyce

Cation-π Interactions in Biomolecular Contexts by Neutron Scattering and Molecular Dynamics: A Case Study of the Tetramethylammonium Cation

Popis výsledku anglicky

Cation−π interactions involving the tetramethylammonium motif are prevalent in biological systems, playing crucial roles in membrane protein function, DNA expression regulation, and protein folding. However, accurately modeling cation−π interactions where electronic polarization plays a critical role is computationally challenging, especially in large biomolecular systems. This study implements a physically justified electronic continuum correction (ECC) to the CHARMM36 force field, scaling ionic charges by a factor of 0.75 to effectively account for electronic polarization without additional computational overhead. This approach, while not specifically designed for cation−π interactions, is shown here to significantly improve predictions of the structure of an aqueous tetramethylammonium–pyridine complex as compared to neutron diffraction data. This result, together with computational predictions for the structure of the aqueous tetramethylammonium–phenol complex, underscores the potential of ECC as a versatile method to improve the description of cation−π interactions in biomolecular simulations.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2025

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Journal of Physical Chemistry B

ISSN

1520-6106

e-ISSN

1520-5207

Svazek periodika

129

Číslo periodika v rámci svazku

27

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

8

Strana od-do

6911-6918

Kód UT WoS článku

001518560100001

EID výsledku v databázi Scopus

2-s2.0-105009270681