Search results for "Simulation."

showing 10 items of 4779 documents

A potential solution to avoid overdose of mixed drugs in the event of Covid-19: Nanomedicine at the heart of the Covid-19 pandemic.

2021

Since 2020, the world is facing the first global pandemic of 21st century. Among all the solutions proposed to treat this new strain of coronavirus, named SARS-CoV-2, the vaccine seems a promising way but the delays are too long to be implemented quickly. In the emergency, a dual therapy has shown its effectiveness but has also provoked a set of debates around the dangerousness of a particular molecule, hydroxychloroquine. In particular, the doses to be delivered, according to the studies, were well beyond the acceptable doses to support the treatment without side effects. We propose here to use all the advantages of nanovectorization to address this question of concentration. Using quantum…

Protein Conformation alpha-HelicalComputer science02 engineering and technologyAzithromycinDrug Delivery SystemsPandemicMaterials ChemistryDrug Dosage CalculationsSpectroscopymedia_common0303 health sciencesEvent (computing)021001 nanoscience & nanotechnologyComputer Graphics and Computer-Aided DesignMolecular Docking SimulationNanomedicineRisk analysis (engineering)Spike Glycoprotein CoronavirusDensity functional theory calculationsNanomedicineThermodynamicsNitrogen OxidesAngiotensin-Converting Enzyme 20210 nano-technologyHydroxychloroquineProtein BindingDrugBoron CompoundsCoronavirus disease 2019 (COVID-19)media_common.quotation_subjectSevere acute respiratory syndrome coronavirus 2 (SARS-CoV-2)Molecular Dynamics SimulationAntiviral AgentsArticle03 medical and health sciencesHumansProtein Interaction Domains and MotifsDual therapyPhysical and Theoretical Chemistry030304 developmental biologyDrug transportBinding SitesSARS-CoV-2Molecular dynamics simulationsCOVID-19NanostructuresCOVID-19 Drug TreatmentKineticsQuantum TheoryProtein Conformation beta-StrandNanovectorizationJournal of molecular graphicsmodelling
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Thermal Isomerization Mechanism in Dronpa and Its Mutants.

2016

The photoswitching speed of the reversibly switchable fluorescent proteins (RSFPs) from the family of green fluorescent proteins (GFPs) changes upon mutation which is of direct importance for various high-resolution techniques. Dronpa is one of the most used RSFPs. Its point mutants rsFastLime (Dronpa V157G) and rsKame (Dronpa V157L) exhibit a striking difference in their photoswitching speed. Here the QM/MM on-the-fly string method is used in order to explore the details of the thermal isomerization mechanism. The four principal ways in which isomerization may occur have been scrutinized for each of the three proteins. It has been shown that thermal isomerization occurs via a one-bond-flip…

Protein Conformation alpha-HelicalMutantGreen Fluorescent ProteinsGlycineMolecular Dynamics Simulation010402 general chemistryPhotochemistry01 natural sciencesQM/MMDronpaIsomerismLeucine0103 physical sciencesThermalMaterials ChemistryPoint MutationPhysical and Theoretical Chemistrychemistry.chemical_classification010304 chemical physicsChemistryTemperatureValineChromophoreFluorescence0104 chemical sciencesSurfaces Coatings and FilmsAmino acidKineticsThermodynamicsIsomerizationThe journal of physical chemistry. B
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Extracellular loop 2 of G protein-coupled olfactory receptors is critical for odorant recognition

2021

International audience; G protein-coupled olfactory receptors (ORs) enable us to detect innumerous odorants. They are also ectopically expressed in non-olfactory tissues and emerging as attractive drug targets. ORs can be promiscuous or highly specific, which is part of a larger mechanism for odor discrimination. Here, we demonstrate that the OR extracellular loop 2 (ECL2) plays critical roles in OR promiscuity and specificity. Using site-directed mutagenesis and molecular modeling, we constructed 3D OR models in which ECL2 forms a lid over the orthosteric pocket. We demonstrate using molecular dynamics simulations that ECL2 controls the shape and the volume of the odorant-binding pocket, m…

Protein Conformation alpha-HelicalOdorant bindingG protein[SDV]Life Sciences [q-bio]Mutagenesis (molecular biology technique)Molecular Dynamics SimulationLigandsReceptors OdorantBiochemistryMice[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyExtracellularOlfactory receptorAnimalsHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyReceptorMolecular BiologyG protein-coupled receptorVirtual screeningmolecular modelingChemistryCell Biologyvirtual screeningLigand (biochemistry)Cell biology[SDV] Life Sciences [q-bio]Smell[SDV.AEN] Life Sciences [q-bio]/Food and NutritionOdorantsMutagenesis Site-Directedsite-directed mutagenesis[SDV.AEN]Life Sciences [q-bio]/Food and Nutrition
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Molecular dynamics studies on Mdm2 complexes: An analysis of the inhibitor influence

2012

p53 is a powerful anti-tumoral molecule frequently inactivated by mutations or deletions in cancer. However, half of all human tumors expresses wild-type p53, and its activation, by antagonizing its negative regulator Mdm2, might offer a new strategy for therapeutic protocol. In this work, we present a molecular dynamics study on Mdm2 structure bound to two different known inhibitors with the aim to investigate the structural transitions between apo-Mdm2 and Mdm2-inhibitor complexes. We tried to gain information about conformational changes binding a benzodiazepine derivative inhibitor with respect the known nutlin and the apo form. The conformational changes alter the size of the cleft and…

Protein ConformationBiophysicsMolecular Dynamics SimulationMdm2 p53 nutlin benzodiazepine Molecular DynamicsBiochemistryNegative regulatorBenzodiazepineschemistry.chemical_compoundMolecular dynamicsHumansMoleculeEnzyme InhibitorsMolecular BiologyBinding SitesbiologyChemistryProto-Oncogene Proteins c-mdm2Cell BiologyNutlinSettore CHIM/08 - Chimica FarmaceuticaBiochemistryDrug DesignBiophysicsbiology.proteinMdm2LinkerBiochemical and Biophysical Research Communications
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Getting Docking into Shape Using Negative Image-Based Rescoring

2019

The failure of default scoring functions to ensure virtual screening enrichment is a persistent problem for the molecular docking algorithms used in the structure-based drug discovery. To remedy this problem, elaborate rescoring and post-processing schemes have been developed with a varying degree of success, specificity, and cost. The negative imagebased rescoring (R-NiB) has been shown to improve the flexible docking performance markedly with a variety of drug targets.The yield improvement is achieved by comparing the alternative docking poses against the negative image of the target protein’s ligand-binding cavity. In other words, the shape and electrostatics of the binding pocket is dir…

Protein ConformationComputer scienceGeneral Chemical EngineeringDrug Evaluation PreclinicalBinding pocketLibrary and Information SciencesCrystallography X-RayMachine learningcomputer.software_genre01 natural sciencesArticledrugsAutodock vinaUser-Computer InterfaceDOCK0103 physical sciencesVirtual screening010304 chemical physicsbusiness.industryDrug discoveryGeneral Chemistrymolecular dockingPANTHER/ShaEP-based R-NiB methodologyAutoDock0104 chemical sciencesComputer Science ApplicationsMolecular Docking SimulationBenchmarking010404 medicinal & biomolecular chemistryDocking (molecular)Artificial intelligencebusinesscomputer
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Efficient computation of root mean square deviations under rigid transformations

2013

The computation of root mean square deviations (RMSD) is an important step in many bioinformatics applications. If approached naively, each RMSD computation takes time linear in the number of atoms. In addition, a careful implementation is required to achieve numerical stability, which further increases runtimes. In practice, the structural variations under consideration are often induced by rigid transformations of the protein, or are at least dominated by a rigid component. In this work, we show how RMSD values resulting from rigid transformations can be computed in constant time from the protein's covariance matrix, which can be precomputed in linear time. As a typical application scenar…

Protein ConformationCovariance matrixComputationComputational BiologyProteinsGeometryGeneral ChemistryRoot mean squareComputational MathematicsComputer SimulationStatistical physicsCluster analysisConstant (mathematics)Time complexityRigid transformationMathematicsNumerical stabilityJournal of Computational Chemistry
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Sequence Determines Degree of Knottedness in a Coarse-Grained Protein Model

2015

Knots are abundant in globular homopolymers but rare in globular proteins. To shed new light on this long-standing conundrum, we study the influence of sequence on the formation of knots in proteins under native conditions within the framework of the hydrophobic-polar (HP) lattice protein model. By employing large scale Wang-Landau simulations combined with suitable Monte Carlo trial moves we show that, even though knots are still abundant on average, sequence introduces large variability in the degree of self-entanglements. Moreover, we are able to design sequences which are either almost always or almost never knotted. Our findings serve as proof of concept that the introduction of just o…

Protein ConformationFOS: Physical sciencesGeneral Physics and AstronomyCondensed Matter - Soft Condensed Matterstomatognathic systemComputer SimulationMathematicsSequence (medicine)chemistry.chemical_classificationQuantitative Biology::BiomoleculesDegree (graph theory)Proteinsfood and beveragesBiomolecules (q-bio.BM)Knot theoryAmino acidsurgical procedures operativeModels ChemicalQuantitative Biology - BiomoleculeschemistryFOS: Biological sciencesProtein modelSoft Condensed Matter (cond-mat.soft)Biological systemHydrophobic and Hydrophilic InteractionsMonte Carlo MethodPhysical Review Letters
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Conformational clamping by a membrane ligand activates the EphA2 receptor

2021

AbstractThe EphA2 receptor is a promising drug target for cancer treatment, since EphA2 activation can inhibit metastasis and tumor progression. It has been recently described that the TYPE7 peptide activates EphA2 using a novel mechanism that involves binding to the single transmembrane domain of the receptor. TYPE7 is a conditional transmembrane (TM) ligand, which only inserts into membranes at neutral pH in the presence of the TM region of EphA2. However, how membrane interactions can activate EphA2 is not known. We systematically altered the sequence of TYPE7 to identify the binding motif used to activate EphA2. With the resulting six peptides, we performed biophysical and cell migratio…

Protein ConformationSequence HomologyTm ligandsPeptideMolecular Dynamics SimulationLigandsReceptor tyrosine kinaseArticleBimolecular fluorescence complementationProtein DomainsStructural BiologyCell MovementCell surface receptorTumor Cells CulturedHumansAmino Acid SequenceReceptorMolecular BiologyMelanomachemistry.chemical_classificationBinding SitesMembranesbiologyChemistryReceptor EphA2Membrane ProteinsLigand (biochemistry)Peptide FragmentsTransmembrane proteinTransmembrane domainMembranebiology.proteinBiophysicsProtein MultimerizationProtein Binding
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Reconstructing the free-energy landscape of Met-enkephalin using dihedral principal component analysis and well-tempered metadynamics

2013

Well-Tempered Metadynamics (WTmetaD) is an efficient method to enhance the reconstruction of the free-energy surface of proteins. WTmetaD guarantees a faster convergence in the long time limit in comparison with the standard metadynamics. It still suffers however from the same limitation, i.e. the non trivial choice of pertinent collective variables (CVs). To circumvent this problem, we couple WTmetaD with a set of CVs generated from a dihedral Principal Component Analysis (dPCA) on the Ramachadran dihedral angles describing the backbone structure of the protein. The dPCA provides a generic method to extract relevant CVs built from internal coordinates. We illustrate the robustness of this …

Protein ConformationSurface PropertiesEnkephalin MethionineFOS: Physical sciencesGeneral Physics and AstronomyDihedral angle01 natural scienceslaw.invention03 medical and health scienceslaw0103 physical sciencesComputer SimulationCartesian coordinate systemPhysics - Biological PhysicsStatistical physicsPhysical and Theoretical ChemistryProtein secondary structureReference modelComputingMilieux_MISCELLANEOUS030304 developmental biologyMathematicsPrincipal Component AnalysisQuantitative Biology::Biomolecules0303 health sciences010304 chemical physicsMetadynamicsEnergy landscapeBiomolecules (q-bio.BM)Condensed Matter - Other Condensed Matter[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryQuantitative Biology - BiomoleculesBiological Physics (physics.bio-ph)FOS: Biological sciencesPrincipal component analysis[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistryPhysics::Accelerator PhysicsThermodynamicsEnergy MetabolismAlgorithmsOther Condensed Matter (cond-mat.other)Ramachandran plot
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Protein Thermal Denaturation and Matrix Glass Transition in Different Protein−Trehalose−Water Systems

2011

Biopreservation by saccharides is a widely studied issue due to its scientific and technological importance; in particular, ternary amorphous protein-saccharide-water systems are extensively exploited to model the characteristics of the in vivo biopreservation process. We present here a differential scanning calorimetry (DSC) study on amorphous trehalose-water systems with embedded different proteins (myoglobin, lysozyme, BSA, hemoglobin), which differ for charge, surface, and volume properties. In our study, the protein/trehalose molar ratio is kept constant at 1/40, while the water/sugar molar ratio is varied between 2 and 300; results are compared with those obtained for binary trehalose…

Protein DenaturationdenaturationMolecular Dynamics SimulationPhase TransitionDSCMatrix (chemical analysis)Hemoglobinschemistry.chemical_compoundDifferential scanning calorimetryMaterials ChemistryAnimalsglass transitionPhysical and Theoretical ChemistrytrehaloseSettore CHIM/02 - Chimica FisicaChromatographyCalorimetry Differential ScanningMyoglobinTemperatureProteinsWaterSerum Albumin BovineTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Surfaces Coatings and FilmsAmorphous solidchemistryChemical engineeringMyoglobinconfinementCattleMuramidaseLysozymeTernary operationGlass transitionThe Journal of Physical Chemistry B
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