Water-tryptophan interactions: lone-pair-pi or O-H-pi? Molecular dynamics simulations of beta-galactosidase suggest that both modes can co-exist
The result's identifiers
Result code in 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>
Result on the web
<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>
Alternative languages
Result language
angličtina
Original language name
Water-tryptophan interactions: lone-pair-pi or O-H-pi? Molecular dynamics simulations of beta-galactosidase suggest that both modes can co-exist
Original language description
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.
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
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2018
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Chemistry - A European Journal
ISSN
0947-6539
e-ISSN
1521-3765
Volume of the periodical
24
Issue of the periodical within the volume
22
Country of publishing house
DE - GERMANY
Number of pages
11
Pages from-to
5849-5859
UT code for WoS article
000430168500021
EID of the result in the Scopus database
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