Search results for "Potential of mean force"

showing 10 items of 19 documents

Adaptive Finite Temperature String Method in Collective Variables.

2017

Here we present a modified version of the on-the-fly string method for the localization of the minimum free energy path in a space of arbitrary collective variables. In the proposed approach the shape of the biasing potential is controlled by only two force constants, defining the width of the potential along the string and orthogonal to it. The force constants and the distribution of the string nodes are optimized during the simulation, improving the convergence. The optimized parameters can be used for umbrella sampling with a path CV along the converged string as the reaction coordinate. We test the new method with three fundamentally different processes: chloride attack to chloromethane…

010304 chemical physicsChemistryString (computer science)Mathematical analysis010402 general chemistry01 natural sciences0104 chemical sciencesReaction coordinateDistribution (mathematics)0103 physical sciencesPath (graph theory)Convergence (routing)Range (statistics)Physical and Theoretical ChemistryUmbrella samplingPotential of mean forceThe journal of physical chemistry. A
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A quantum mechanics-molecular mechanics study of dissociative electron transfer : The methylchloride radical anion in aqueous solution

2002

The dissociative electron transfer reaction CH3Cl+e−→CH3•+Cl− in aqueous solution is studied by using a QM/MM method. In this work the quantum subsystem (a methylchloride molecule plus an electron) is described using density functional theory while the solvent (300 water molecules) is described using the TIP3P classical potential. By means of molecular dynamics simulations and the thermodynamic integration technique we obtained the potential of mean force (PMF) for the carbon–chlorine bond dissociation of the neutral and radical anion species. Combining these two free energy curves we found a quadratic dependence of the activation free energy on the reaction free energy in agreement with Ma…

Aqueous solutionChemistryGeneral Physics and AstronomyThermodynamic integrationFree radicalsMolecular dynamics methodOrganic compounds ; Dissociation ; Charge exchange ;Free radicals ; Negative ions ; Molecular dynamics method ; Digital simulationKinetic energyNegative ionsUNESCO::FÍSICA::Química físicaMolecular dynamicsElectron transferQuantum mechanicsOrganic compoundsMoleculeDensity functional theoryPhysical and Theoretical ChemistryPotential of mean forcePhysics::Chemical PhysicsCharge exchangeDigital simulation:FÍSICA::Química física [UNESCO]Dissociation
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Mapping the network of pathways of CO diffusion in myoglobin.

2010

The pathways of diffusion of a CO molecule inside a myoglobin protein and toward the solvent are investigated. Specifically, the three-dimensional potential of mean force (PMF or free energy) of the CO molecule position inside the protein is calculated by using the single-sweep method in concert with fully resolved atomistic simulations in explicit solvent. The results are interpreted under the assumption that the diffusion of the ligand can be modeled as a navigation on the PMF in which the ligand hops between the PMF local minima following the minimum free energy paths (MFEPs) with rates set by the free energy barriers that need to be crossed. Here, all the local minima of the PMF, the MF…

Carbon MonoxideMyoglobinCo diffusionimulationGeneral ChemistryBiochemistryCatalysisMaxima and minimaDiffusionCrystallographychemistry.chemical_compoundColloid and Surface ChemistryMyoglobinchemistryChemical physicsDocking (molecular)MoleculeThermodynamicsComputer SimulationPotential of mean forceBinding siteMinimum free energyJournal of the American Chemical Society
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Can hydrophobic interactions be correctly reproduced by the continuum models?

1996

The ability of the continuum models to describe hydrophobic interactions is investigated. In this work we have studied the interactions between two methane molecules in aqueous solution by means of a continuum model. The resulting potential of mean force is in good agreement with those obtained using Monte Carlo and molecular dynamics techniques. The three energy contributions appearing in the continuum energy partition (electrostatic, dispersion−repulsion, and cavitation) have been analyzed. The cavitation free energy plays the most important role of the three, determining the existence of an energy barrier between the contact minimum and the separated methane monomers. This barrier, which…

Continuum (measurement)ChemistryMonte Carlo methodGeneral EngineeringMethaneHydrophobic effectMolecular dynamicschemistry.chemical_compoundClassical mechanicsChemical physicsCavitationMoleculePhysics::Chemical PhysicsPhysical and Theoretical ChemistryPotential of mean force
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Comparative Study of the Mechanical Unfolding Pathways of α- and β-Peptides

2015

Using molecular simulations, we analyze the unfolding pathways of various peptides. We compare the mechanical unfolding of a β-alanine's octamer (β-HAla8) and an α-alanine's decamer (α-Ala10). Using force-probe molecular-dynamics simulations, to induce unfolding, we show that the 3(14)-helix formed by β-HAla8 is mechanically more stable than the α-helix formed by α-Ala10, although both structures are stabilized by six hydrogen bonds. Additionally, computations of the potential of mean force validate this result and show that also the thermal stability of the 3(14)-helix is higher. It is demonstrated that β-HAla8 unfolds in a two-step fashion with a stable intermediate. This is contrasted wi…

Dynamic strengthHydrogen bondHydrogen BondingMolecular Dynamics SimulationProtein Structure SecondarySurfaces Coatings and Filmschemistry.chemical_compoundCrystallographyMonomerchemistrybeta-AlanineMaterials ChemistryBiophysicsThermal stabilityHistone octamerPhysical and Theoretical ChemistryPotential of mean forcePeptidesThe Journal of Physical Chemistry B
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Physics and biophysics of solvent induced forces: hydrophobic interactions and context-dependent hydration

1998

Solvent induced forces (SIFs) among solutes derive from solvent structural modification due to solutes, and consequent thermodynamic drive towards minimization of related free energy costs. The role of SIFs in biomolecular conformation and function is appreciated by observing that typical SIF values fall within the 20–200 pN interval, and that proteins are stable by only a few kcal mol–1 (1 kcal mol–1 corresponds to 70 pN A). Here we study SIFs, in systems of increasing complexity, using Molecular Dynamics (MD) simulations which give time- and space-resolved details on the biologically significant scale of single protein residues and sidechains. Of particular biological relevance among our …

Folding (chemistry)Hydrophobic effectMolecular dynamicsMolecular recognitionChemistryChemical physicsComputational chemistryBiophysicsContext (language use)Charge (physics)General MedicinePotential of mean forceElectric chargeEuropean Biophysics Journal
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Thermodynamics of hydronium and hydroxide surface solvation.

2014

[Introduction] The concentration of hydronium and hydroxide at the water-air interface has been under debate for a long time. Recent evidence from a range of experiments and theoretical calculations strongly suggests the water surface is somewhat acidic. Using novel polarizable models we have performed potential of mean force calculations of a hydronium ion, a hydroxide ion and a water molecule in a water droplet and a water slab and we were able to rationalize that hydronium, but not hydroxide, is slightly enriched at the surface for two reasons. First, because the hydrogen-bond acceptance capacity of hydronium is weaker than water it is more favorable to have the hydronium oxygen on the s…

HydroniumhydroxidekemiaInorganic chemistryThermodynamics010402 general chemistry01 natural sciencesIonSurface tensionchemistry.chemical_compound0103 physical scienceshydroksoniumPotential of mean forcePhysics::Chemical Physicsta116thermodynamiikka010304 chemical physicsHydrogen bondSolvationGeneral Chemistryhydronium0104 chemical scienceschemistry13. Climate actiontermodynamiikkaddc:540hydroksidiHydroxideSelf-ionization of water
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Molecular structure and multi-body potential of mean force in silica-polystyrene nanocomposites

2018

We perform a systematic application of the hybrid particle-field molecular dynamics technique [Milano et al, J. Chem. Phys. 2009, 130, 214106] to study interfacial properties and potential of mean force (PMF) for separating nanoparticles (NPs) in a melt. Specifically, we consider Silica NPs bare or grafted with Polystyrene chains, aiming to shed light on the interactions among free and grafted chains affecting the dispersion of NPs in the nanocomposite. The proposed hybrid models show good performances in catching the local structure of the chains, and in particular their density profiles, documenting the existence of the "wet-brush-to-dry-brush" transition. By using these models, the PMF b…

Materials scienceGrafting (chemical)Composite numberPhase separationNanoparticleFOS: Physical sciences02 engineering and technologyMolecular dynamicsCondensed Matter - Soft Condensed Matter010402 general chemistry01 natural sciencesNanocompositeschemistry.chemical_compoundMolecular dynamicsGrafting (chemical) Molecular dynamics Nanocomposites Phase separation Plasma interactions SilicaPhysics - Chemical PhysicsMoleculeGeneral Materials SciencePotential of mean forceChemical Physics (physics.chem-ph)NanocompositePlasma interactionsSilicaComputational Physics (physics.comp-ph)021001 nanoscience & nanotechnology0104 chemical scienceschemistryChemical engineeringSoft Condensed Matter (cond-mat.soft)Polystyrene0210 nano-technologyDispersion (chemistry)Physics - Computational Physics
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Membrane-mediated Protein-protein Interaction: A Monte Carlo Study

2012

We investigate membrane-mediated interactions between transmembrane proteins using coarse-grained models. We compare the effective potential of mean force (PMF) between two proteins, which are always aligned parallel to the z-axis of the simulation box, with those PMFs obtained for proteins with fluctuating orientations. The PMFs are dominated by an oscillatory packing-driven contribution and a smooth attractive hydrophobic mismatch contribution, which vanishes if the hydrophobic length of the protein matches the thickness of the membrane. If protein orientations are allowed to fluctuate, the oscillations are greatly reduced compared to proteins with fixed orientation. Furthermore, the hydr…

PhysicsPhysics::Biological PhysicsQuantitative Biology::BiomoleculesMonte Carlo methodBiomedical EngineeringFOS: Physical sciencesPharmaceutical ScienceMedicine (miscellaneous)BioengineeringCondensed Matter - Soft Condensed MatterTransmembrane proteinProtein–protein interactionQuantitative Biology::Subcellular ProcessesHydrophobic mismatchMembraneBiological Physics (physics.bio-ph)Chemical physicsMonolayerSoft Condensed Matter (cond-mat.soft)Physics - Biological PhysicsPotential of mean forceLipid bilayerBiotechnologyCurrent Nanoscience
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Mapping CO diffusion paths in Myoglobin with the Single Sweep Method

2010

The pathways of diffusion and escape of a CO molecule inside and out a myoglobin protein are investigated. Specifically, the three-dimensional potential of mean force (PMF or free energy) of the CO molecule position inside the protein is calculated by using the single-sweep method in concert with fully resolved atomistic simulations in explicit solvent.The results are interpreted under the assumption that the diffusion of the ligand can be modeled as a navigation on the PMF in which the ligand hops between the PMF local minima following the minimum free energy paths (MFEPs) with rates set by the free energy barriers that need to be crossed. We calculate all these quantities --local minima, …

Physics::Biological PhysicsQuantitative Biology::BiomoleculesCo diffusionBiophysicsMolecular physicsMaxima and minimachemistry.chemical_compoundCrystallographyMyoglobinchemistrymyoglobin free energyDocking (molecular)MoleculeSingle sweepBinding sitePotential of mean force
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