Search results for "molecular dynamics simulation"

showing 10 items of 260 documents

Non-equilibrium Markov state modeling of periodically driven biomolecules

2019

Molecular dynamics simulations allow to study the structure and dynamics of single biomolecules in microscopic detail. However, many processes occur on time scales beyond the reach of fully atomistic simulations and require coarse-grained multiscale models. While systematic approaches to construct such models have become available, these typically rely on microscopic dynamics that obey detailed balance. In vivo, however, biomolecules are constantly driven away from equilibrium in order to perform specific functions and thus break detailed balance. Here we introduce a method to construct Markov state models for systems that are driven through periodically changing one (or several) external p…

Computer scienceFOS: Physical sciencesGeneral Physics and AstronomyMarkov processMolecular Dynamics Simulation010402 general chemistry01 natural sciencesMolecular dynamicssymbols.namesake0103 physical sciencesPhysics - Biological PhysicsStatistical physicsPhysical and Theoretical ChemistryCondensed Matter - Statistical Mechanicschemistry.chemical_classificationQuantitative Biology::BiomoleculesStatistical Mechanics (cond-mat.stat-mech)010304 chemical physicsMarkov chainBiomoleculeMolecular biophysicsDetailed balanceDipeptidesComputational Physics (physics.comp-ph)Markov Chains0104 chemical sciencesModels ChemicalchemistryBiological Physics (physics.bio-ph)Benchmark (computing)symbolsState (computer science)Physics - Computational PhysicsThe Journal of Chemical Physics
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Comparative classical and ab initio Molecular Dynamics study of molten and glassy germanium dioxide

2008

A Molecular Dynamics (MD) study of static and dynamic properties of molten and glassy germanium dioxide is presented. The interactions between the atoms are modelled by the classical pair potential proposed by Oeffner and Elliott (OE) [Oeffner R D and Elliott S R 1998, Phys. Rev. B, 58, 14791]. We compare our results to experiments and previous simulations. In addition, an ab initio method, the so-called Car-Parrinello Molecular Dynamics (CPMD), is applied to check the accuracy of the structural properties, as obtained by the classical MD simulations with the OE potential. As in a similar study for SiO2, the structure predicted by CPMD is only slightly softer than that resulting from the cl…

Condensed Matter - Materials ScienceGermanium dioxideCar–Parrinello molecular dynamicsMaterials scienceDynamic structure factorRelaxation (NMR)Ab initioMaterials Science (cond-mat.mtrl-sci)FOS: Physical sciencesThermodynamicsDisordered Systems and Neural Networks (cond-mat.dis-nn)Condensed Matter - Disordered Systems and Neural NetworksCondensed Matter Physicschemistry.chemical_compoundMolecular dynamicsgermaniamolecular dynamics simulationchemistryAb initio quantum chemistry methodsGeneral Materials SciencePair potential
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Controlling Exciton Propagation in Organic Crystals through Strong Coupling to Plasmonic Nanoparticle Arrays.

2022

Exciton transport in most organic materials is based on an incoherent hopping process between neighboring molecules. This process is very slow, setting a limit to the performance of organic optoelectronic devices. In this Article, we overcome the incoherent exciton transport by strongly coupling localized singlet excitations in a tetracene crystal to confined light modes in an array of plasmonic nanoparticles. We image the transport of the resulting exciton–polaritons in Fourier space at various distances from the excitation to directly probe their propagation length as a function of the exciton to photon fraction. Exciton–polaritons with an exciton fraction of 50% show a propagation length…

Condensed Matter::Quantum GasesCondensed Matter::OtherPhysics::Opticsmolecular dynamics simulationspolariton transportfysikaalinen kemiaCondensed Matter::Mesoscopic Systems and Quantum Hall EffectelektronitkvasihiukkasetplasmonicsAtomic and Molecular Physics and Opticsnanoparticle arraytetraceneElectronic Optical and Magnetic MaterialsCondensed Matter::Materials Sciencemolekyylifysiikkaplasmoniikkastrong light-matter couplingeksitonitnanohiukkasetmolekyylidynamiikkaElectrical and Electronic EngineeringBiotechnologyACS photonics
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The Study of Carbamoyl Phosphate Synthetase 1 Deficiency Sheds Light on the Mechanism for Switching On/Off the Urea Cycle

2015

12 páginas, 4 figuras, 2 tablas.

Conformational changeCarbamoyl-Phosphate Synthase I Deficiency DiseaseAllosteric regulationCarbamoyl-Phosphate Synthase (Ammonia)Urea cycle diseases610 Medicine & healthBiologyMolecular Dynamics Simulationurologic and male genital diseases03 medical and health sciences0302 clinical medicineGlutamates1311 GeneticsAmmoniaEnzyme StabilityGeneticsmedicine1312 Molecular BiologyHumansUreaHyperammonemiaSite-directed mutagenesisMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesSite-directed mutagenesisurogenital systemMutagenesisCarbamoyl phosphate synthetase 1HyperammonemiaCarbamoyl phosphate synthetasemedicine.diseaseAllosteric regulation3. Good healthProtein Structure TertiaryRestrained molecular dynamicsKineticsEnzymeBiochemistrychemistry10036 Medical ClinicEnzymeUrea cycleMutationInborn errors030217 neurology & neurosurgerySignal Transduction
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Decipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.

2013

ATP regulates the function of many proteins in the cell by transducing its binding and hydrolysis energies into protein conformational changes by mechanisms which are challenging to identify at the atomic scale. Based on molecular dynamics (MD) simulations, a method is proposed to analyze the structural changes induced by ATP binding to a protein by computing the effective free-energy landscape (FEL) of a subset of its coordinates along its amino-acid sequence. The method is applied to characterize the mechanism by which the binding of ATP to the nucleotide-binding domain (NBD) of Hsp70 propagates a signal to its substrate-binding domain (SBD). Unbiased MD simulations were performed for Hsp…

Conformational changeProtein ConformationAllosteric regulationPlasma protein bindingMolecular Dynamics SimulationCellular and Molecular NeuroscienceProtein structureAdenosine TriphosphateGeneticsHSP70 Heat-Shock ProteinsMolecular Biologylcsh:QH301-705.5Nuclear Magnetic Resonance BiomolecularEcology Evolution Behavior and SystematicsEcologybiologyChemistryEscherichia coli ProteinsEnergy landscapeComputational Theory and MathematicsBiochemistrylcsh:Biology (General)Docking (molecular)Modeling and SimulationChaperone (protein)Biophysicsbiology.proteinBinding domainProtein BindingResearch ArticlePLoS computational biology
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Phase Behavior of Active Swimmers in Depletants: Molecular Dynamics and Integral Equation Theory

2013

We study the structure and phase behavior of a binary mixture where one of the components is self-propelling in nature. The inter-particle interactions in the system were taken from the Asakura-Oosawa model, for colloid-polymer mixtures, for which the phase diagram is known. In the current model version the colloid particles were made active using the Vicsek model for self-propelling particles. The resultant active system was studied by molecular dynamics methods and integral equation theory. Both methods produce results consistent with each other and demonstrate that the Vicsek model based activity facilitates phase separation, thus broadening the coexistence region.

Current (mathematics)PolymersMovementFOS: Physical sciencesGeneral Physics and AstronomyBinary numberCondensed Matter - Soft Condensed MatterMolecular Dynamics SimulationModels BiologicalDiffusionMolecular dynamicsColloidPhase (matter)ColloidsStatistical physicsCondensed Matter - Statistical MechanicsPhase diagramPhysicsStatistical Mechanics (cond-mat.stat-mech)Active systemsModels TheoreticalIntegral equationCondensed Matter::Soft Condensed MatterKineticsClassical mechanicsModels ChemicalSoft Condensed Matter (cond-mat.soft)Physical Review Letters
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Comparison of virtual high-throughput screening methods for the identification of phosphodiesterase-5 inhibitors.

2011

Reliable and effective virtual high-throughput screening (vHTS) methods are desperately needed to minimize the expenses involved in drug discovery projects. Here, we present an improvement to the negative image-based (NIB) screening: the shape, the electrostatics, and the solvation state of the target protein’s ligand-binding site are included into the vHTS. Additionally, the initial vHTS results are postprocessed with molecular mechanics/generalized Born surface area (MMGBSA) calculations to estimate the favorability of ligand-protein interactions. The results show that docking produces very good early enrichment for phosphodiesterase-5 (PDE-5); however, in general, the NIB and the ligand-…

Cyclic Nucleotide Phosphodiesterases Type 5Virtual screeningHigh-Throughput Screening MethodsDrug discoveryChemistryGeneral Chemical EngineeringHigh-throughput screeningMedical screeningStatic ElectricityDrug Evaluation PreclinicalNanotechnologyGeneral ChemistryComputational biologyLibrary and Information SciencesMolecular Dynamics SimulationPhosphodiesterase 5 InhibitorsLigandsComputer Science ApplicationsHigh-Throughput Screening AssaysSubstrate SpecificityUser-Computer InterfaceDocking (molecular)Catalytic DomainJournal of chemical information and modeling
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Enhancement of premature stop codon readthrough in the CFTR gene by Ataluren (PTC124) derivatives.

2015

Abstract Premature stop codons are the result of nonsense mutations occurring within the coding sequence of a gene. These mutations lead to the synthesis of a truncated protein and are responsible for several genetic diseases. A potential pharmacological approach to treat these diseases is to promote the translational readthrough of premature stop codons by small molecules aiming to restore the full-length protein. The compound PTC124 (Ataluren) was reported to promote the readthrough of the premature UGA stop codon, although its activity was questioned. The potential interaction of PTC124 with mutated mRNA was recently suggested by molecular dynamics (MD) studies highlighting the importanc…

Cystic FibrosisNonsense mutationPeptide Chain Elongation TranslationalCystic Fibrosis Transmembrane Conductance RegulatorSettore BIO/11 - Biologia MolecolareMolecular Dynamics SimulationCFTR genechemistry.chemical_compoundStructure-Activity RelationshipPlasmidDrug DiscoveryTumor Cells CulturedCoding regionHumansGreen fluorescent proteinGenePharmacologyGeneticsMessenger RNAOxadiazolesNonsense mutationDose-Response Relationship DrugMolecular StructureDrug Discovery3003 Pharmaceutical ScienceOrganic ChemistryTranslational readthroughSettore CHIM/06 - Chimica OrganicaGeneral MedicinePTCs readthroughStop codonAtalurenSettore BIO/18 - GeneticachemistrySettore CHIM/03 - Chimica Generale E InorganicaCodon NonsenseCystic fibrosiMutationFluorinated oxadiazoleHeLa CellsEuropean journal of medicinal chemistry
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Post-Translational Regulation of CYP450s Metabolism As Revealed by All-Atoms Simulations of the Aromatase Enzyme.

2019

Phosphorylation by kinases enzymes is a widespread regulatory mechanism able of rapidly altering the function of target proteins. Among these are cytochrome P450s (CYP450), a superfamily of enzymes performing the oxidation of endogenous and exogenous substrates thanks to the electron supply of a redox partner. In spite of its pivotal role, the molecular mechanism by which phosphorylation modulates CYP450s metabolism remains elusive. Here by performing microsecond-long all-atom molecular dynamics simulations, we disclose how phosphorylation regulates estrogen biosynthesis, catalyzed by the Human Aromatase (HA) enzyme. Namely, we unprecedentedly propose that HA phosphorylation at Y361 markedl…

CytochromeFlavin MononucleotideProtein ConformationGeneral Chemical EngineeringFlavin mononucleotide-Oxidative phosphorylationLibrary and Information SciencesMolecular Dynamics Simulation01 natural scienceschemistry.chemical_compoundAromatase0103 physical sciencesPost-translational regulationAromatasePhosphorylationBinding Sites010304 chemical physicsbiologyKinaseGeneral ChemistryMetabolism0104 chemical sciencesComputer Science ApplicationsCell biology010404 medicinal & biomolecular chemistrychemistrySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteinFlavin-Adenine DinucleotidePhosphorylationQuantum TheoryProtein Processing Post-TranslationalNADPJournal of chemical information and modeling
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All-Atom simulations disclose how cytochrome reductase reshapes the substrate access/egress routes of its partner cyp450s

2020

Cytochromes P450 enzymes (CYP450s) promote the oxidative metabolism of a variety of substrates via the electrons supplied by the cytochrome P450 reductase (CPR) and upon formation of a CPR/CYP450 adduct. In spite of the pivotal regulatory importance of this process, the impact of CPR binding on the functional properties of its partner CYP450 remains elusive. By performing multiple microsecond-long all-Atom molecular dynamics simulations of a 520â »000-Atom model of a CPR/CYP450 adduct embedded in a membrane mimic, we disclose the molecular terms for their interactions, considering the aromatase (HA) enzyme as a proxy of the CYP450 family. Our study strikingly unveils that CPR binding alters…

CytochromeStereochemistryeducationPlasma protein binding-ReductaseMolecular Dynamics Simulation010402 general chemistry01 natural sciencesSubstrate SpecificityElectron Transport03 medical and health sciencesAromataseCytochrome P-450 Enzyme Systemhealth services administrationHumansddc:530General Materials Sciencecardiovascular diseasesP450 EnzymesPhysical and Theoretical Chemistryhealth care economics and organizations030304 developmental biologyNADPH-Ferrihemoprotein Reductase0303 health sciencesOxidative metabolismbiologyChemistrySubstrate (chemistry)Cytochrome P450 reductaseElectron transport chain0104 chemical sciencesAromatase; Cytochrome P-450 Enzyme System; Electron Transport; Humans; Molecular Dynamics Simulation; NADPH-Ferrihemoprotein Reductase; Protein Binding; Substrate SpecificitySettore CHIM/03 - Chimica Generale E Inorganicabiology.proteintherapeuticsProtein Binding
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