Search results for "molecular dynamics simulation"

showing 10 items of 260 documents

Critical Structural Defects Explain Filamin A Mutations Causing Mitral Valve Dysplasia

2019

Mitral valve diseases affect approximately 3% of the population and are the most common reasons for valvular surgery because no drug-based treatments exist. Inheritable genetic mutations have now been established as the cause of mitral valve insufficiency, and four different missense mutations in the filamin A gene (FLNA) have been found in patients suffering from non-syndromic mitral valve dysplasia (MVD). The FLNA protein is expressed, in particular, in endocardial endothelia during fetal valve morphogenesis and is key in cardiac development. The FLNA-MVD causing mutations are clustered in the N-terminal region of FLNA. How the mutations in FLNA modify its structure and function, have mos…

Protein FoldingdysplasiatFilamins[SDV]Life Sciences [q-bio]PopulationProtein Tyrosine Phosphatase Non-Receptor Type 12BiophysicsMutation Missensesynnynnäiset sydänviatProtein tyrosine phosphataseBiologyMolecular Dynamics Simulationmedicine.disease_causeFilamin03 medical and health sciences0302 clinical medicinemitral valve dysplasiaMitral valvemedicineFLNAMissense mutationHumanseducationGene030304 developmental biologyGenetics0303 health sciencesMutationeducation.field_of_studyBinding SitesMitral Valve Prolapsecritical structural defectshiippaläppäfilamiinitArticles3. Good healthmedicine.anatomical_structurecardiovascular systemfilamin A mutationsgeneettiset tekijätmutaatiot030217 neurology & neurosurgeryProtein Binding
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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Targeting SARS-CoV-2 RBD Interface: a Supervised Computational Data-Driven Approach to Identify Potential Modulators

2020

Coronavirus disease 2019 (COVID-19) has spread out as a pandemic threat affecting over 2 million people. The infectious process initiates via binding of SARS-CoV-2 Spike (S) glycoprotein to host angiotensin-converting enzyme 2 (ACE2). The interaction is mediated by the receptor-binding domain (RBD) of S glycoprotein, promoting host receptor recognition and binding to ACE2 peptidase domain (PD), thus representing a promising target for therapeutic intervention. Herein, we present a computational study aimed at identifying small molecules potentially able to target RBD. Although targeting PPI remains a challenge in drug discovery, our investigation highlights that interaction between SARS-CoV…

Protein domainPneumonia ViralDruggabilityDrug Evaluation Preclinicalprotein-protein interactionsComputational biologyBiologyMolecular Dynamics SimulationPeptidyl-Dipeptidase AMolecular dynamics01 natural sciencesBiochemistryMolecular Docking SimulationAntiviral Agentsdockingmolecular dynamicProtein–protein interactionSmall Molecule LibrariesBetacoronavirusProtein DomainsDrug DiscoveryHumansGeneral Pharmacology Toxicology and PharmaceuticsPandemicsPharmacologyFull Paperpharmacophore010405 organic chemistryDrug discoverySARS-CoV-2Organic ChemistryCOVID-19Small molecule0104 chemical sciencesProtein-Protein InteractionMolecular Docking Simulation010404 medicinal & biomolecular chemistryDocking (molecular)Spike Glycoprotein CoronavirusdockingMolecular MedicineAngiotensin-Converting Enzyme 2PharmacophoreCoronavirus InfectionsProtein Binding
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Investigation of Phosphorylation-Induced Folding of an Intrinsically Disordered Protein by Coarse-Grained Molecular Dynamics

2021

Apart from being the most common mechanism of regulating protein function and transmitting signals throughout the cell, phosphorylation has an ability to induce disorder-to-order transition in an intrinsically disordered protein. In particular, it was shown that folding of the intrinsically disordered protein, eIF4E-binding protein isoform 2 (4E-BP2), can be induced by multisite phosphorylation. Here, the principles that govern the folding of phosphorylated 4E-BP2 (pT37pT46 4E-BP2(18–62)) are investigated by analyzing canonical and replica exchange molecular dynamics trajectories, generated with the coarse-grained united-residue force field, in terms of local and global motions and the time…

Protein isoformPhysicsProtein functionProtein Folding010304 chemical physicsMolecular Dynamics Simulation01 natural sciencesForce field (chemistry)ArticleComputer Science ApplicationsFolding (chemistry)Standing waveIntrinsically Disordered Proteinssymbols.namesakeMolecular dynamicsChemical physics0103 physical sciencessymbolsPhosphorylationThermodynamicsPhysical and Theoretical ChemistryPhosphorylationNonlinear Schrödinger equation
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Charge-Neutral Constant pH Molecular Dynamics Simulations Using a Parsimonious Proton Buffer

2016

In constant pH molecular dynamics simulations, the protonation states of titratable sites can respond to changes of the pH and of their electrostatic environment. Consequently, the number of protons bound to the biomolecule, and therefore the overall charge of the system, fluctuates during the simulation. To avoid artifacts associated with a non-neutral simulation system, we introduce an approach to maintain neutrality of the simulation box in constant pH molecular dynamics simulations, while maintaining an accurate description of all protonation fluctuations. Specifically, we introduce a proton buffer that, like a buffer in experiment, can exchange protons with the biomolecule enabling its…

ProtonprotonationAnalytical chemistryProtonationBuffersMolecular Dynamics Simulation010402 general chemistry01 natural sciencesBuffer (optical fiber)Molecular dynamics0103 physical sciencesPhysical and Theoretical ChemistryNuclear Experimentta116chemistry.chemical_classificationQuantitative Biology::Biomolecules010304 chemical physicspHQuantitative Biology::Molecular NetworksBiomoleculeProteinsCharge (physics)molecular dynamics simulationselectrostatic environmentHydrogen-Ion Concentration0104 chemical sciencesComputer Science ApplicationschemistryChemical physicsThermodynamicsTitrationbufferProtonsConstant (mathematics)Journal of Chemical Theory and Computation
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Mechanical unfolding pathway of a model β-peptide foldamer.

2015

Foldamers constructed from oligomers of β-peptides form stable secondary helix structures already for small chain lengths, which makes them ideal candidates for the investigation of the (un)folding of polypeptides. Here, the results of molecular simulations of the mechanical unfolding of a β-heptapeptide in methanol solvent revealing the detailed unfolding pathway are reported. The unfolding process is shown to proceed via a stable intermediate even for such a small system. This result is arrived at performing non-equilibrium force ramp simulations employing different pulling velocities and also using standard calculations of the potential of mean force, i.e., the free energy as a function …

Quantitative Biology::BiomoleculesChemistryMethanolEquilibrium unfoldingFoldamerGeneral Physics and AstronomyEnergy landscapeThermodynamicsHydrogen BondingMolecular Dynamics SimulationKinetic energyProtein Structure SecondaryFolding (chemistry)CrystallographyKineticsHelixSolventsPhysical and Theoretical ChemistryPotential of mean forceChemical equilibriumPeptidesProtein UnfoldingThe Journal of chemical physics
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Solvent-induced free energy landscape and solute-solvent dynamic coupling in a multielement solute

1999

AbstractMolecular dynamics simulations using a simple multielement model solute with internal degrees of freedom and accounting for solvent-induced interactions to all orders in explicit water are reported. The potential energy landscape of the solute is flat in vacuo. However, the sole untruncated solvent-induced interactions between apolar (hydrophobic) and charged elements generate a rich landscape of potential of mean force exhibiting typical features of protein landscapes. Despite the simplicity of our solute, the depth of minima in this landscape is not far in size from free energies that stabilize protein conformations. Dynamical coupling between configurational switching of the syst…

Quantitative Biology::BiomoleculesProtein ConformationChemistryBiophysicsDegrees of freedom (physics and chemistry)ProteinsEnergy landscapeMolecular Dynamics SimulationSolventMolecular dynamicsCoupling (computer programming)Chemical physicsComputational chemistrySolventsThermodynamicsProtein foldingPotential of mean forceHydrophobic and Hydrophilic InteractionsOrder of magnitudeResearch Article
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A combined molecular dynamics and Monte Carlo study of the approach towards phase separation in colloid-polymer mixtures.

2011

A coarse-grained model for colloid-polymer mixtures is investigated where both colloids and polymer coils are represented as point-like particles interacting with spherically symmetric effective potentials. Colloid-colloid and colloid-polymer interactions are described by Weeks-Chandler-Andersen potentials, while the polymer-polymer interaction is very soft, of strength k(B)T/2 for maximum polymer-polymer overlap. This model can be efficiently simulated both by Monte Carlo and molecular dynamics methods, and its phase diagram closely resembles that of the well-known Asakura-Oosawa model. The static and dynamic properties of the model are presented for systems at critical colloid density, va…

RENORMALIZATIONPolymersMonte Carlo methodBiophysicsThermodynamicsSOFT MATTERMolecular Dynamics SimulationDiffusionColloidMolecular dynamicsFLUIDSCritical point (thermodynamics)PARTICLESGeneral Materials ScienceComputer SimulationColloidsAnisotropyPhase diagramchemistry.chemical_classificationQuantitative Biology::BiomoleculesModels StatisticalChemistryPhysicsPolymerCondensed Matter PhysicsCondensed Matter::Soft Condensed MatterShear rateKineticsSIMULATIONPERTURBATION-THEORYAnisotropyStress MechanicalPAIR POTENTIALSMonte Carlo MethodBEHAVIORINTERFACESAlgorithmsJournal of physics. Condensed matter : an Institute of Physics journal
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Unveiling the reaction mechanism of novel copper N-alkylated tetra-azacyclophanes with outstanding superoxide dismutase activity.

2020

Quantum chemical and multiscale calculations reveal the mechanistic pathway of two superoxide dismutase mimetic N-alkylated tetra-azacyclophane copper complexes with remarkable activity. The arrangement of the binding site afforded by the bulky alkyl substituents and the coordinated water molecule as a proton source play key roles in the reaction mechanism.

Reaction mechanismAlkylationStereochemistrychemistry.chemical_elementAlkylationMolecular Dynamics SimulationCrystallography X-RayCatalysisSuperoxide dismutaseCoordination ComplexesEthers CyclicMaterials ChemistryMoleculeHumansBinding siteAlkylchemistry.chemical_classificationbiologySuperoxide DismutaseMetals and AlloysGeneral Chemistrybiology.organism_classificationCopperSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryCeramics and Compositesbiology.proteinTetraQuantum Theorylipids (amino acids peptides and proteins)CopperChemical communications (Cambridge, England)
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Computational simulations on the binding and reactivity of a nitrile inhibitor of the SARS-CoV-2 main protease.

2021

We present a detailed computational analysis of the binding mode and reactivity of the novel oral inhibitor PF-07321332 developed against the SARS-CoV-2 3CL protease. Alchemical free energy calculations suggest that positions P3 and P4 could be susceptible to improvement in order to get a larger binding strength. QM/MM simulations unveil the reaction mechanism for covalent inhibition, showing that the nitrile warhead facilitates the recruitment of a water molecule for the proton transfer step.

Reaction mechanismNitrileLactamsProlineStereochemistrymedicine.medical_treatmentMolecular Dynamics SimulationCatalysischemistry.chemical_compoundMolecular dynamicsLeucineCatalytic DomainNitrilesMaterials ChemistrymedicineMoleculeHumansReactivity (chemistry)Protease InhibitorsBinding siteCoronavirus 3C ProteasesProteaseBinding SitesSARS-CoV-2Metals and AlloysCOVID-19General ChemistrySurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialschemistryCovalent bondCeramics and CompositesQuantum TheoryThermodynamicsChemical communications (Cambridge, England)
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