Water-tryptophan interactions: lone-pair-pi or O-H-pi? Molecular dynamics simulations of beta-galactosidase suggest that both modes can co-exist

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14310%2F18%3A00100777" target="_blank" >RIV/00216224:14310/18:00100777 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1002/chem.201705364" target="_blank" >http://dx.doi.org/10.1002/chem.201705364</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/chem.201705364" target="_blank" >10.1002/chem.201705364</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Water-tryptophan interactions: lone-pair-pi or O-H-pi? Molecular dynamics simulations of beta-galactosidase suggest that both modes can co-exist

Popis výsledku v původním jazyce

In proteins, the indole side-chain of tryptophan can interact with water molecules either in-plane, forming H-bonds, or out-of-plane, with the water molecule contacting the aromatic pi-face. The latter interaction can be either of the lone-pair---pi (lp---pi) type or correspond to the O-H---pi binding mode, an ambiguity that X-ray structures usually do not resolve. Here we report molecular dynamics (MD) simulations of a solvated beta-galactosidase monomer which illustrate how a water molecule located at the pi-face of an indole side-chain of tryptophan can adapt to the position of proximate residues and "select" its binding mode. In one such site, the water molecule is predicted to rapidly oscillate between the O-H---pi and lp---pi binding modes, gaining thus entropic advantage. Our MD simulations provide support for the role of lp---pi interactions in the stabilization of protein structures.

Název v anglickém jazyce

Water-tryptophan interactions: lone-pair-pi or O-H-pi? Molecular dynamics simulations of beta-galactosidase suggest that both modes can co-exist

Popis výsledku anglicky

In proteins, the indole side-chain of tryptophan can interact with water molecules either in-plane, forming H-bonds, or out-of-plane, with the water molecule contacting the aromatic pi-face. The latter interaction can be either of the lone-pair---pi (lp---pi) type or correspond to the O-H---pi binding mode, an ambiguity that X-ray structures usually do not resolve. Here we report molecular dynamics (MD) simulations of a solvated beta-galactosidase monomer which illustrate how a water molecule located at the pi-face of an indole side-chain of tryptophan can adapt to the position of proximate residues and "select" its binding mode. In one such site, the water molecule is predicted to rapidly oscillate between the O-H---pi and lp---pi binding modes, gaining thus entropic advantage. Our MD simulations provide support for the role of lp---pi interactions in the stabilization of protein structures.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

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OECD FORD obor

10403 - Physical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

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

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Chemistry - A European Journal

ISSN

0947-6539

e-ISSN

1521-3765

Svazek periodika

24

Číslo periodika v rámci svazku

22

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

11

Strana od-do

5849-5859

Kód UT WoS článku

000430168500021

EID výsledku v databázi Scopus

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