Search results for "Molecular Dynamic"

showing 10 items of 1090 documents

Mechanistic insights into the phosphoryl transfer reaction in cyclin-dependent kinase 2: a QM/MM study

2019

AbstractCyclin-dependent kinase 2 (CDK2) is an important member of the CDK family exerting its most important function in the regulation of the cell cycle. It catalyzes the transfer of the gamma phosphate group from an ATP (adenosine triphosphate) molecule to a Serine/Threonine residue of a peptide substrate. Due to the importance of this enzyme, and protein kinases in general, a detailed understanding of the reaction mechanism is desired. Thus, in this work the phosphoryl transfer reaction catalyzed by CDK2 was revisited and studied by means of hybrid quantum mechanics/molecular mechanics (QM/MM) calculations. Our results show that the base-assisted mechanism is preferred over the substrat…

Models MolecularComposite ParticlesProtein ConformationPhysical ChemistryBiochemistry01 natural sciencesSubstrate Specificitychemistry.chemical_compoundPhosphorylationPost-Translational ModificationFree Energy0303 health sciencesMultidisciplinarybiologyKinasePhysicsQChemical ReactionsRChemistryReaction DynamicsPhysical SciencesThermodynamicsMedicineProtonsResearch ArticleChemical ElementsAtomsStereochemistryScienceMolecular Dynamics Simulation010402 general chemistryMolecular mechanicsReactantsQM/MMStructure-Activity Relationship03 medical and health sciencesCyclin-dependent kinaseParticle PhysicsNuclear PhysicsNucleons030304 developmental biologyChemical BondingCyclin-Dependent Kinase 2Cyclin-dependent kinase 2Biology and Life SciencesProteinsActive siteHydrogen BondingTransition StateBond order0104 chemical sciencesOxygenModels Chemicalchemistrybiology.proteinQuantum TheoryAdenosine triphosphate
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Unraveling the role of protein dynamics in dihydrofolate reductase catalysis

2013

Protein dynamics have controversially been proposed to be at the heart of enzyme catalysis, but identification and analysis of dynamical effects in enzyme-catalyzed reactions have proved very challenging. Here, we tackle this question by comparing an enzyme with its heavy ((15)N, (13)C, (2)H substituted) counterpart, providing a subtle probe of dynamics. The crucial hydride transfer step of the reaction (the chemical step) occurs more slowly in the heavy enzyme. A combination of experimental results, quantum mechanics/molecular mechanics simulations, and theoretical analyses identify the origins of the observed differences in reactivity. The generally slightly slower reaction in the heavy e…

Models MolecularComputational chemistryStereochemistryKineticsBiophysicsMolecular Dynamics SimulationTritiumCatalysisEnzyme catalysisReaction coordinateReaction rateMolecular dynamicsQuantum biologyEscherichia coliReactivity (chemistry)Carbon IsotopesQuantum biologyMultidisciplinaryNitrogen IsotopesChemistryProtein dynamicsBiological chemistryProteinsTetrahydrofolate DehydrogenaseKineticsChemical physicsPhysical Sciences
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Self-assembly of janus dendrimers into uniform dendrimersomes and other complex architectures

2010

Janus Drug Delivery Vehicle Efficient drug delivery vehicles need to be produced in a limited size range and with uniform size distribution. The self-assembly of traditional small-molecule and polymeric amphiphiles has led to the production of micelles, liposomes, polymeric micelles, and polymersomes for use in drug delivery applications. Now, Percec et al. (p. 1009 ) describe the self-assembly of Janus-type (i.e., two-headed) dendrimers to produce monodisperse supramolecular constructs, termed “dendrimersomes,” and other complex architectures. The structures, which showed long-term stability as well as very narrow size distributions, were easily produced by the injection of an ethanolic so…

Models MolecularDendrimersMaterials scienceSurface Propertiesta221Complex ArchitecturesNanotechnologyMolecular Dynamics SimulationSurface-Active AgentsBiomimetic MaterialsDendrimerAmphiphileJanusta218LiposomeDrug Carriersta214MultidisciplinaryAntibiotics Antineoplasticta114Molecular StructureVesicleCryoelectron MicroscopyWaterMembranes ArtificialNanostructuresJanus DendrimersSelf-AssemblyMembraneUniform DendrimersomesDoxorubicinPolymersomeSelf-assemblyHydrophobic and Hydrophilic InteractionsScience
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Role of Solvent on Nonenzymatic Peptide Bond Formation Mechanisms and Kinetic Isotope Effects

2013

Based on the hypothesis that similar mechanisms are involved in the peptide bond formation in aqueous solution and in the ribosome, the aminolysis of esters in aqueous solution has been the subject of numerous studies as the reference reaction for the catalyzed process. The mechanisms proposed in the literature have been explored in the present paper by hybrid QM/MM molecular dynamics simulations. The free energy profiles have been computed with the QM region of the system described at semiempirical AM1 level and by DFT within the M06-2X functional. According to the results, the formation of adduct zwitterion species is a preliminary step required for all possible mechanisms. Then, from dif…

Models MolecularEster aminolysisMolecular Dynamics SimulationMethyl formateBiochemistryCatalysisMolecular dynamicschemistry.chemical_compoundColloid and Surface ChemistryAminolysisIsotopesComputational chemistryKinetic isotope effectOrganic chemistryPeptide bondConformational isomerismDensity functionalsChemistryAqueous-solutionGeneral ChemistryHydrazinolysisRibosomeTransition stateKineticsSolvation shellChorismate mutaseZwitterionSolventsTransition-state structuresPeptides
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Molecular dynamics studies on HIV-1 protease: a comparison of the flap motions between wild type protease and the M46I/G51D double mutant

2007

The emergence of drug-resistant mutants of HIV-1 is a tragic effect associated with conventional long-treatment therapies against acquired immunodeficiency syndrome. These mutations frequently involve the aspartic protease encoded by the virus; knowledge of the molecular mechanisms underlying the conformational changes of HIV-1 protease mutants may be useful in developing more effective and longer lasting treatment regimes. The flap regions of the protease are the target of a particular type of mutations occurring far from the active site. These mutations modify the affinity for both substrate and ligands, thus conferring resistance. In this work, molecular dynamics simulations were perform…

Models MolecularGromacs 3.2Anti-HIV AgentsProtein Conformationmedicine.medical_treatmentflap motionMutantCatalysisVirusInorganic ChemistryProtein structureHIV ProteaseHIV-1 proteaseDrug Resistance ViralEnzyme StabilityHIV-1 proteasemedicineHumansComputer SimulationPhysical and Theoretical Chemistrychemistry.chemical_classificationProteasebiologyHIV-1 drug-resistant mutantOrganic ChemistryWild typeActive siteRecombinant ProteinsComputer Science ApplicationsCell biologyEnzymemolecular dynamics simulationAmino Acid SubstitutionComputational Theory and MathematicsBiochemistrychemistryMutationHIV-1biology.protein
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A Structural Model of the Human α7 Nicotinic Receptor in an Open Conformation

2015

International audience; Nicotinic acetylcholine receptors (nAchRs) are ligand-gated ion channels that regulate chemical transmission at the neuromuscular junction. Structural information is available at low resolution from open and closed forms of an eukaryotic receptor, and at high resolution from other members of the same structural family, two prokaryotic orthologs and an eukary- otic GluCl channel. Structures of human channels however are still lacking. Homology modeling and Molecular Dynamics simulations are valuable tools to predict structures of unknown proteins, however, for the case of human nAchRs, they have been unsuccessful in providing a stable open structure so far. This is du…

Models MolecularHydrogen bondingalpha7 Nicotinic Acetylcholine ReceptorProtein ConformationMolecular Sequence DataMESH: Sequence Alignmentligand gated ion channles molecular dynamics simulation epibatidine waterlcsh:MedicineSequence alignmentMESH: Amino Acid SequenceMolecular Dynamics SimulationMESH: Models Molecular*Molecular dynamicsProtein structureSequence alignmentCationsHumansMESH: Molecular Dynamics SimulationHomology modelingAmino Acid SequenceNicotinic Receptorlcsh:ScienceBiochemical simulationsIon channelAcetylcholine receptorIonsMESH: Protein Conformation*MultidisciplinaryMESH: HumansMESH: Molecular Sequence DataChemistryMESH: Protein Multimerizationlcsh:RMESH: alpha7 Nicotinic Acetylcholine Receptor/chemistry*[SDV.BIBS]Life Sciences [q-bio]/Quantitative Methods [q-bio.QM]Transmembrane proteinSimulation and modelingNicotinic agonistBiochemistryBiophysicsProtein structurelcsh:QProtein MultimerizationResearch ArticleStructural Model
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Molecular dynamics simulation of sucrose- and trehalose-coated carboxy-myoglobin

2005

We performed a room temperature molecular dynamics (MD) simulation on a system containing 1 carboxy-myoglobin (MbCO) molecule in a sucrose–water matrix of identical composition (89% [sucrose/(sucrose + water)] w/w) as for a previous trehalose–water–MbCO simulation (Cottone et al., Biophys J 2001;80:931–938). Results show that, as for trehalose, the amplitude of protein atomic mean-square fluctuations, on the nanosecond timescale, is reduced with respect to aqueous solutions also in sucrose. A detailed comparison as a function of residue number evidences mobility differences along the protein backbone, which can be related to a different efficacy in bioprotection. Different heme pocket struc…

Models MolecularInfrared spectroscopyDisaccharidesBiochemistrychemistry.chemical_compoundMolecular dynamicsStructural BiologyCarbohydrate ConformationMoleculeComputer Simulationheme pocket; hydrogen bond; mean-square fluctuations; protein dynamics; sucrose; trehaloseheme pocketMolecular Biologytrehalosehydrogen bondAqueous solutionBinding SitesHydrogen bondMyoglobinProtein dynamicssucroseTrehaloseCrystallographyKineticschemistryMyoglobinprotein dynamicsmolecular dynamics myoglobin disaccharidemean-square fluctuations
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Modulation of Structural Heterogeneity Controls Phytochrome Photoswitching

2019

Phytochromes sense red/far-red light and control many biological processes in plants, fungi, and bacteria. Although crystal structures of dark and light adapted states have been determined, the molecular mechanisms underlying photoactivation remains elusive. Here we demonstrate that the conserved tongue region of the PHY domain of a 57kDa photosensory module of Deinococcus radiodurans phytochrome, changes from a structurally heterogeneous dark state to an ordered light activated state. The results were obtained in solution by utilizing a laser-triggered activation approach detected on the atomic level with high-resolution protein NMR spectroscopy. The data suggest that photosignaling of phy…

Models MolecularLightTongue regionBiophysicsphototransduction03 medical and health sciences0302 clinical medicineProtein DomainsPHYmolekyylidynamiikkaprotein structureNMR-spektroskopiaNuclear Magnetic Resonance Biomolecular030304 developmental biologyphytochrome0303 health sciencesPhytochromebiologyChemistryProtein NMR SpectroscopyDeinococcus radioduransArticlesDarknessbiology.organism_classificationmolecular dynamicsNMRStructural heterogeneityDark stateModulationBiophysicsvalokemiaproteiinitDeinococcusPhytochrome030217 neurology & neurosurgeryBiophysical Journal
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Mechanically interlocked calix[4]arene dimers display reversible bond breakage under force.

2009

The physics of nanoscopic systems is strongly governed by thermal fluctuations that produce significant deviations from the behaviour of large ensembles1,2. Stretching experiments of single molecules offer a unique way to study fundamental theories of statistical mechanics, as recently shown for the unzipping of RNA hairpins3. Here, we report a molecular design based on oligo calix[4]arene catenanes—calixarene dimers held together by 16 hydrogen bridges—in which loops within the molecules limit how far the calixarene nanocapsules can be separated. This mechanically locked structure tunes the energy landscape of dimers, thus permitting the reversible rupture and rejoining of the individual n…

Models MolecularMacromolecular SubstancesSurface PropertiesBiomedical EngineeringMolecular ConformationThermal fluctuationsBioengineeringNanotechnologyMolecular dynamicsPhenolsCalixareneMaterials TestingMoleculeNanotechnologyGeneral Materials ScienceComputer SimulationElectrical and Electronic EngineeringParticle SizePhysicsHydrogen bondEnergy landscapeStatistical mechanicsPhysicistCondensed Matter PhysicsAtomic and Molecular Physics and OpticsNanostructuresModels ChemicalChemical physicsStress MechanicalCalixarenesCrystallizationDimerizationNature nanotechnology
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Influence of Whole-Body Dynamics on 15N PISEMA NMR Spectra of Membrane Proteins: A Theoretical Analysis

2009

AbstractMembrane proteins and peptides exhibit a preferred orientation in the lipid bilayer while fluctuating in an anisotropic manner. Both the orientation and the dynamics have direct functional implications, but motions are usually not accessible, and structural descriptions are generally static. Using simulated data, we analyze systematically the impact of whole-body motions on the peptide orientations calculated from two-dimensional polarization inversion spin exchange at the magic angle (PISEMA) NMR. Fluctuations are found to have a significant effect on the observed spectra. Nevertheless, wheel-like patterns are still preserved, and it is possible to determine the average peptide til…

Models MolecularMagic angleRotationGaussianLipid BilayersNormal DistributionBiophysicsMolecular physicsProtein Structure SecondarySpectral lineQuantitative Biology::Subcellular ProcessesMolecular dynamicssymbols.namesakeNuclear magnetic resonanceOrientationComputer SimulationLipid bilayerAnisotropyNuclear Magnetic Resonance BiomolecularQuantitative Biology::BiomoleculesChemistryMembranePolarization (waves)AmplitudesymbolsDimyristoylphosphatidylcholinePeptidesBiophysical Journal
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