Changes in the hydration structure of imidazole upon protonation: Neutron scattering and molecular simulations

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00475774" target="_blank" >RIV/61388963:_____/17:00475774 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1063/1.4982937" target="_blank" >http://dx.doi.org/10.1063/1.4982937</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1063/1.4982937" target="_blank" >10.1063/1.4982937</a>

Result language

angličtina

Original language name

Changes in the hydration structure of imidazole upon protonation: Neutron scattering and molecular simulations

Original language description

The imidazole motif is widely encountered in biomolecules, and its biological role, for instance, as a proton relay, is often linked to its ability to form hydrogen bonds with water molecules. The detailed characterization of the hydration pattern of imidazole and of its changes upon protonation is thus of high interest. Here, we combine neutron scattering experiments with force field simulations to provide an unprecedented characterization of the neutral and protonated imidazole solvation at the atomistic level. We show that neutron diffraction data can be used to assess the quality of the imidazole force field in molecular simulations. Simulations using the CHARMM general force field for imidazole are in excellent agreement with the experimental neutron scattering data and we use them to provide an atomic scale interpretation of the neutron scattering patterns. Upon protonation, we clearly identify the signature of the reorganization in the hydration pattern caused by the change from one H-bond donor and one H-bond acceptor group for imidazole to two H-bond donor groups for imidazolium. We also point the limits of the experiment, which are rather insensitive to details of the H-bond geometry at the deprotonated nitrogen of imidazole and further complement the description of the hydration structure with ab initio molecular dynamics simulations.

Czech name

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Czech description

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Type

J_imp - 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

Project

<a href="/en/project/GBP208%2F12%2FG016" target="_blank" >GBP208/12/G016: Controlling structure and function of biomolecules at the molecular scale: theory meets experiment</a><br>

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2017

Confidentiality

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

Name of the periodical

Journal of Chemical Physics

ISSN

0021-9606

e-ISSN

—

Volume of the periodical

146

Issue of the periodical within the volume

18

Country of publishing house

US - UNITED STATES

Number of pages

11

Pages from-to

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UT code for WoS article

000401368900039

EID of the result in the Scopus database

2-s2.0-85019186151