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@ARTICLE{Tarenzi:861313,
author = {Tarenzi, Thomas and Calandrini, Vania and Potestio,
Raffaello and Carloni, Paolo},
title = {{O}pen-{B}oundary {M}olecular
{M}echanics/{C}oarse-{G}rained {F}ramework for {S}imulations
of {L}ow-{R}esolution {G}-{P}rotein-{C}oupled
{R}eceptor–{L}igand {C}omplexes},
journal = {Journal of chemical theory and computation},
volume = {15},
number = {3},
issn = {1549-9626},
address = {Washington, DC},
reportid = {FZJ-2019-01806},
pages = {2101–2109},
year = {2019},
abstract = {G-protein-coupled receptors (GPCRs) constitute as much as
$30\%$ of the overall proteins targeted by FDA-approved
drugs. However, paucity of structural experimental
information and low sequence identity between members of the
family impair the reliability of traditional docking
approaches and atomistic molecular dynamics simulations for
in silico pharmacological applications. We present here a
dual-resolution approach tailored for such low-resolution
models. It couples a hybrid molecular
mechanics/coarse-grained (MM/CG) scheme, previously
developed by us for GPCR–ligand complexes, with a
Hamiltonian-based adaptive resolution scheme (H-AdResS) for
the solvent. This dual-resolution approach removes
potentially inaccurate atomistic details from the model
while building a rigorous statistical ensemble—the grand
canonical one—in the high-resolution region. We validate
the method on a well-studied GPCR–ligand complex, for
which the 3D structure is known, against atomistic
simulations. This implementation paves the way for future
accurate in silico studies of low-resolution ligand/GPCRs
models.},
cin = {IAS-5 / INM-9},
ddc = {610},
cid = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
pnm = {574 - Theory, modelling and simulation (POF3-574)},
pid = {G:(DE-HGF)POF3-574},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:30763087},
UT = {WOS:000461533000052},
doi = {10.1021/acs.jctc.9b00040},
url = {https://juser.fz-juelich.de/record/861313},
}