Search results for "molecular dynamics"

showing 10 items of 1075 documents

Combined use of 13C chemical shift and 1H alpha-13C alpha heteronuclear NOE data in monitoring a protein NMR structure refinement.

1995

A large portion of the 13C resonance assignments for murine epidermal growth factor (mEGF) at pH 3.1 and 28 degrees C has been determined at natural isotope abundance. Sequence-specific 13C assignments are reported for 100% of the assignable C alpha, 96% of the C beta, 86% of the aromatic and 70% of the remaining peripheral aliphatic resonances of mEGF. A good correlation was observed between experimental and back-calculated C alpha chemical shifts for regions of regular beta-sheet structure. These assignments also provide the basis for interpreting 1H alpha-13C alpha heteronuclear NOE (HNOE) values in mEGF at natural isotope abundance. Some of the backbone polypeptide segments with high in…

Models MolecularProtein FoldingMagnetic Resonance SpectroscopyProtein ConformationMolecular Sequence DataAlpha (ethology)Natural abundanceBiochemistryProtein Structure SecondaryMolecular dynamicsMiceProtein structureAnimalsAmino Acid SequenceBinding siteSpectroscopyCarbon IsotopesEpidermal Growth FactorMolecular StructureChemistryChemical shiftResonanceProteinsCrystallographyHeteronuclear moleculeThermodynamicsHydrogenJournal of biomolecular NMR
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A human CCT5 gene mutation causing distal neuropathy impairs hexadecamer assembly in an archaeal model

2014

Chaperonins mediate protein folding in a cavity formed by multisubunit rings. The human CCT has eight non-identical subunits and the His147Arg mutation in one subunit, CCT5, causes neuropathy. Knowledge is scarce on the impact of this and other mutations upon the chaperone's structure and functions. To make progress, experimental models must be developed. We used an archaeal mutant homolog and demonstrated that the His147Arg mutant has impaired oligomeric assembly, ATPase activity, and defective protein homeostasis functions. These results establish for the first time that a human chaperonin gene defect can be reproduced and studied at the molecular level with an archaeal homolog. The major…

Models MolecularProtein FoldingProtein ConformationProtein subunitMutantMolecular Sequence Datahuman CCT5 gene mutation molecular dynamics neuropathy archaeal modelSequence alignmentGene mutationBiologyArticleChaperonin03 medical and health sciences0302 clinical medicineProtein structureHumansProtein Interaction Domains and MotifsAmino Acid Sequence030304 developmental biologyGenetics0303 health sciencesMultidisciplinarySettore BIO/16 - Anatomia UmanaArchaeaSettore CHIM/08 - Chimica FarmaceuticaChaperone (protein)Mutationbiology.proteinThermodynamicsProtein foldingProtein MultimerizationSequence Alignment030217 neurology & neurosurgeryChaperonin Containing TCP-1
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The amorphous silica-liquid water interface studied by ab initio molecular dynamics (AIMD): local organization in global disorder

2014

International audience; The structural organization of water at a model of amorphous silica-liquid water interface is investigated by ab initio molecular dynamics (AIMD) simulations at room temperature. The amorphous surface is constructed with isolated, H-bonded vicinal and geminal silanols. In the absence of water, the silanols have orientations that depend on the local surface topology (i.e. presence of concave and convex zones). However, in the presence of liquid water, only the strong inter-silanol H-bonds are maintained, whereas the weaker ones are replaced by H-bonds formed with interfacial water molecules. All silanols are found to act as H- bond donors to water. The vicinal silanol…

Models MolecularProtonSurface Propertiesamorphous silicawatergeminal silanols02 engineering and technologyMolecular Dynamics Simulation010402 general chemistry01 natural sciencesAb initio molecular dynamicsComputational chemistryMoleculeGeneral Materials ScienceQuartzGeminalMolecular StructureChemistryab initio molecular dynamicsHydrogen Bonding[CHIM.MATE]Chemical Sciences/Material chemistrySilanes021001 nanoscience & nanotechnologyCondensed Matter PhysicsSilicon Dioxide0104 chemical sciencesAmorphous solidChemical physicsQuantum TheoryAmorphous silicaProtons0210 nano-technologyVicinal
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A3 adenosine receptor: Homology modeling and 3D-QSAR studies

2012

Adenosine receptors (AR) belong to the superfamily of G-protein-coupled receptors (GPCRs). They are divided into four subtypes (A1, A2A, A2B, and A3) [1], and can be distinguished on the basis of their distinct molecular structures, distinct tissues distribution, and selectivity for adenosine analogs [2,3]. The hA3R, the most recently identified adenosine receptor, is involved in a variety of intracellular signaling pathways and physiological functions [4]. Expression of A3R was reported to be elevated in cancerous tissues [5], and A3 antagonists have been proposed for therapeutic treatments of cancer. The recent literature availability of crystal structure of hA2A adenosine receptor (PDB c…

Models MolecularQuantitative structure–activity relationshipReceptor Adenosine A2AAdenosine A3 Receptor AntagonistsQuantitative Structure-Activity RelationshipComputational biologyBiologyPharmacologyDrug DiscoveryMolecular dynamics simulationMaterials ChemistrymedicineHumansAmino Acid SequenceHomology modelingPhysical and Theoretical ChemistryReceptorA3 INHIBITORS HOMOLOGY MODELING 3D-QSARSpectroscopyG protein-coupled receptorA3 ReceptorBinding SitesTriazinesReceptor Adenosine A3Intracellular Signaling Peptides and ProteinsTriazolesA3 ADENOSINE RECEPTORComputer Graphics and Computer-Aided DesignAdenosine receptorAdenosineSettore CHIM/08 - Chimica FarmaceuticaPharmacophoresHomology modellingPharmacophoreProtein Bindingmedicine.drug
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Molecular dynamics simulation of carboxy-myoglobin embedded in a trehalose-water matrix

2001

AbstractWe report on a molecular dynamics (MD) simulation of carboxy-myoglobin (MbCO) embedded in a water-trehalose system. The mean square fluctuations of protein atoms, calculated at different temperatures in the 100–300K range, are compared with those from a previous MD simulation on an H2O-solvated MbCO and with experimental data from Mössbauer spectroscopy and incoherent elastic neutron scattering on trehalose-coated MbCO. The results show that, for almost all the atomic classes, the amplitude of the nonharmonic motions stemming from the interconversion among the protein’s conformational substates is reduced with respect to the H2O-solvated system, and their onset is shifted toward hig…

Models MolecularRange (particle radiation)MyoglobinProtein ConformationIronBiophysicsTrehaloseWaterHemeNeutron scatteringIn Vitro TechniquesTrehaloseMolecular physicsBiophysical Phenomenachemistry.chemical_compoundMolecular dynamicsCrystallographyAmplitudeProtein structureMyoglobinchemistryMössbauer spectroscopyAnimalsThermodynamicsResearch Article
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Promiscuity in alkaline phosphatase superfamily. Unraveling evolution through molecular simulations.

2011

We here present a theoretical study of the alkaline hydrolysis of a phosphodiester (methyl p-nitrophenyl phosphate or MpNPP) in the active site of Escherichia coli alkaline phosphatase (AP), a monoesterase that also presents promiscuous activity as a diesterase. The analysis of our simulations, carried out by means of molecular dynamics (MD) simulations with hybrid quantum mechanics/molecular mechanics (QM/MM) potentials, shows that the reaction takes place through a D(N)A(N) or dissociative mechanism, the same mechanism employed by AP in the hydrolysis of monoesters. The promiscuous activity observed in this superfamily can be then explained on the basis of a conserved reaction mechanism. …

Models MolecularReaction mechanismStereochemistrydnaNAlkaline hydrolysis (body disposal)AlkaliesMolecular Dynamics SimulationBiochemistryMolecular mechanicsCatalysisMolecular dynamicsColloid and Surface ChemistryCatalytic DomainphosphodiesterEscherichia colibiologyChemistryHydrolysisActive siteGeneral ChemistryAlkaline PhosphataseEnzymesEnzyme ActivationPhosphodiester bondbiology.proteinAlkaline phosphataseQuantum Theoryalkaline phosphataseJournal of the American Chemical Society
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Dynamic Effects on Reaction Rates in a Michael Addition Catalyzed by Chalcone Isomerase. Beyond the Frozen Environment Approach

2008

We present a detailed microscopic study of the dynamics of the Michael addition reaction leading from 6'-deoxychalcone to the corresponding flavanone. The reaction dynamics are analyzed for both the uncatalyzed reaction in aqueous solution and the reaction catalyzed by Chalcone Isomerase. By means of rare event simulations of trajectories started at the transition state, we have computed the transmission coefficients, obtaining 0.76 +/- 0.04 and 0.87 +/- 0.03, in water and in the enzyme, respectively. According to these simulations, the Michael addition can be seen as a formation of a new intramolecular carbon-oxygen bond accompanied by a charge transfer essentially taking place from the nu…

Models MolecularReaction ratesMechanicsBiochemistryChemical reactionCatalysisReaction coordinateReaction rateMolecular dynamicsCharge transferChalconesColloid and Surface ChemistryNucleophileComputational chemistryChemical reactionsFreezingIntramolecular LyasesReaction kineticsFourier AnalysisChemistryIntermolecular forceWaterGeneral ChemistryCarbonDynamicsKineticsModels ChemicalReaction dynamicsChemical physicsIntramolecular forceFlavanonesQuantum TheoryThermodynamicsIon exchangeJournal of the American Chemical Society
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Structural and Functional Similarity of Amphibian Constitutive Androstane Receptor with Mammalian Pregnane X Receptor

2016

The nuclear receptors and xenosensors constitutive androstane receptor (CAR, NR1I3) and pregnane X receptor (PXR, NR1I2) induce the expression of xenobiotic metabolizing enzymes and transporters, which also affects various endobiotics. While human and mouse CAR feature a high basal activity and low induction upon ligand exposure, we recently identified two constitutive androstane receptors in Xenopus laevis (xlCARá and â) that possess PXR-like characteristics such as low basal activity and activation in response to structurally diverse compounds. Using a set of complementary computational and biochemical approaches we provide evidence for xlCARá being the structural and functional counterpa…

Models MolecularReceptors SteroidReceptors Cytoplasmic and Nuclearlcsh:MedicineMolecular Dynamics SimulationPharmacologyBiologyCrystallography X-Raydigestive systemAmphibian ProteinsCell LineXenopus laevischemistry.chemical_compoundChlorocebus aethiopsConstitutive androstane receptorCoactivatorAnimalsHumansBinding sitelcsh:ScienceReceptorConstitutive Androstane ReceptorPregnane X receptorBinding SitesMultidisciplinarylcsh:RPregnane X ReceptorCorrectionLigand (biochemistry)digestive system diseasesCell biologychemistryNuclear receptorCOS Cellslcsh:QAndrostanePLOS ONE
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Homology modeling using simulated annealing of restrained molecular dynamics and conformational search calculations with CONGEN: application in predi…

1997

We have developed an automatic approach for homology modeling using restrained molecular dynamics and simulated annealing procedures, together with conformational search algorithms available in the molecular mechanics program CONGEN (Bruccoleri RE, Karplus M, 1987, Biopolymers 26:137-168). The accuracy of the method is validated by "predicting" structures of two homeodomain proteins with known three-dimensional structures, and then applied to predict the three-dimensional structure of the homeodomain of the murine Msx-1 transcription factor. Regions of the unknown protein structure that are highly homologous to the known template structure are constrained by "homology distance constraints,"…

Models MolecularSaccharomyces cerevisiae ProteinsProtein ConformationMSX1 Transcription FactorMolecular Sequence DataSaccharomyces cerevisiaeBiologyProtein EngineeringBiochemistryProtein Structure SecondaryMolecular dynamicsMiceProtein structureAnimalsComputer SimulationHomology modelingAmino Acid SequenceMolecular BiologyHomeodomain ProteinsMSX1 Transcription FactorSequence Homology Amino AcidNuclear ProteinsProtein engineeringProtein superfamilyengrailedRepressor ProteinsCrystallographyAntennapedia Homeodomain ProteinThreading (protein sequence)AlgorithmsInformation SystemsTranscription FactorsResearch ArticleProtein science : a publication of the Protein Society
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Can multiscale simulations unravel the function of metallo-enzymes to improve knowledge-based drug discovery?

2019

Metallo-enzymes are a large class of biomolecules promoting specialized chemical reactions. Quantum-classical quantum mechanics/molecular mechanics molecular dynamics, describing the metal site at quantum mechanics level, while accounting for the rest of system at molecular mechanics level, has an accessible time-scale limited by its computational cost. Hence, it must be integrated with classical molecular dynamics and enhanced sampling simulations to disentangle the functions of metallo-enzymes. In this review, we provide an overview of these computational methods and their capabilities. In particular, we will focus on some systems such as CYP19A1 a Fe-dependent enzyme involved in estroge…

Models MolecularSpliceosomeQM/MM molecular dynamicsProtein ConformationComputer scienceMetallo enzymeComputational biology01 natural sciencesMolecular mechanicsribozymeStructure-Activity Relationship03 medical and health sciencesMolecular dynamicsMM molecular dynamicsAromataseCatalytic DomainDrug Discoverysteroid synthesisCYP19A1RNA CatalyticDensity Functional Theory030304 developmental biologyQMPharmacologychemistry.chemical_classificationDNA processing enzymes0303 health sciencesMetallo-proteinsbiologyDrug discoveryBiomoleculeRibozymeDNABiosynthetic PathwaysEnzymes0104 chemical sciences010404 medicinal & biomolecular chemistrychemistrySettore CHIM/03 - Chimica Generale E InorganicaMetalsbiology.proteinRNAThermodynamicsMolecular MedicinespliceosomeFunction (biology)Protein BindingFuture Medicinal Chemistry
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