Search results for "molecular dynamics simulation"

showing 10 items of 260 documents

Closed-Locked and Apo-Resting State Structures of the Human α7 Nicotinic Receptor: A Computational Study

2018

International audience; Nicotinic acetylcholine receptors, belonging to the Cys-loop super-family of ligand-gated ion channels (LGICs), are membrane proteins present in neurons and at neuromuscular junctions. They are responsible for signal transmission, and their function is regulated by neurotransmitters, agonists and antagonists drugs. A detailed knowledge of their conformational transition in response to ligand binding is critical to understand the basis of ligand-receptor interaction, in view of new pharmacological approaches to control receptor activity. However, the scarcity of experimentally derived structures of human channels makes this perspective extremely challenging. To contri…

0301 basic medicinealpha7 Nicotinic Acetylcholine ReceptorProtein ConformationGeneral Chemical EngineeringMolecular Dynamics SimulationLibrary and Information Sciences03 medical and health sciencesMolecular dynamics0302 clinical medicineHumansHomology modelingReceptorIon channelAcetylcholine receptor[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]Protein StabilityChemistryWaterHydrogen BondingGeneral ChemistryLigand (biochemistry)molecular dynamicsComputer Science Applications[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsTransmembrane domain030104 developmental biologyNicotinic agonistBiophysics[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]Conotoxinsligand gated ion channel030217 neurology & neurosurgery
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A possible desensitized state conformation of the human α7 nicotinic receptor: A molecular dynamics study

2017

International audience; The determination of the conformational states corresponding to diverse functional roles of ligand gated ion channels is subject of intense investigation with various techniques, from X-rays structure determination to electrophysiology and computational modeling. Even with a certain number of structures becoming recently available, only few major structural features distinguishing conductive open channel from the non conductive resting protein have been highlighted, while high-resolution details are still missing. The characterization of the desensitized conformation(s) is even more complex, and only few specific characteristics have been identified. Furthermore, exp…

0301 basic medicinealpha7 Nicotinic Acetylcholine ReceptorStereochemistryPyridinesBiophysicsMolecular Dynamics SimulationBiochemistry03 medical and health sciencesMolecular dynamicsmedicineHumansHomology modelingnicotinic receptor epibatidine molecular dynamics inactive stateIon channel[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryProtein StabilityOrganic ChemistryHydrogen BondingBridged Bicyclo Compounds HeterocyclicSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Protein Structure Tertiary[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsElectrophysiology030104 developmental biologyNicotinic agonistα7 nicotinic receptorEpibatidineLigand-gated ion channel[INFO.INFO-BI]Computer Science [cs]/Bioinformatics [q-bio.QM]medicine.drug
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Mechanistic study of the biosynthesis of R-phenylcarbinol by acetohydroxyacid synthase enzyme using hybrid quantum mechanics/molecular mechanics simu…

2021

Abstract The biosynthesis of R-phenylacetylcarbinol (R-PAC) by the acetohydroxy acid synthase, (AHAS) is addressed by molecular dynamics simulations (MD), hybrid quantum mechanics/molecular mechanics (QM/MM), and QM/MM free energy calculations. The results show the reaction starts with the nucleophilic attack of the C2α atom of the HEThDP intermediate on the Cβ atom of the carbonyl group of benzaldehyde substrate via the formation of a transition state (TS1) with the HEThDP intermediate under 4′-aminopyrimidium (APH+) form. The calculated activation free energy for this step is 17.4 kcal mol−1 at 27 °C. From this point, the reaction continues with the abstraction of Hβ atom of the HEThDP in…

0301 basic medicinechemistry.chemical_classification030102 biochemistry & molecular biologyBiophysicsSubstrate (chemistry)Molecular Dynamics SimulationBiochemistryMolecular mechanicsBenzaldehydeAcetolactate Synthase03 medical and health scienceschemistry.chemical_compoundMolecular dynamics030104 developmental biologychemistryCatalytic cycleNucleophileYlideQuantum mechanicsAtomQuantum TheoryMolecular BiologyBenzyl AlcoholsArchives of Biochemistry and Biophysics
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Hydrogen Bond Fluctuations Control Photochromism in a Reversibly Photo-Switchable Fluorescent Protein

2015

Reversibly switchable fluorescent proteins (RSFPs) are essential for high-resolution microscopy of biological samples, but the reason why these proteins are photochromic is still poorly understood. To address this problem, we performed molecular dynamics simulations of the fast switching Met159Thr mutant of the RSFP Dronpa. Our simulations revealed a ground state structural heterogeneity in the chromophore pocket that consists of three populations with one, two, or three hydrogen bonds to the phenolate moiety of the chromophore. By means of non-adiabatic quantum mechanics/molecular dynamics simulations, we demonstrated that the subpopulation with a single hydrogen bond is responsible for of…

0301 basic medicinefluorescent proteinsMolecular Dynamics Simulation010402 general chemistryPhotochemistry01 natural sciencesCatalysis03 medical and health sciencesDronpaMolecular dynamicsPhotochromismIsomerismta116structural heterogeneityHydrogen bondChemistryRational designHydrogen BondingGeneral MedicineGeneral ChemistryChromophorePhotochemical Processeslaskennallinen kemiaphotochromismcomputational chemistryFluorescence0104 chemical sciencesLuminescent Proteins030104 developmental biologyQuantum Theoryphoto-isomerizationIsomerizationAngewandte Chemie International Edition
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Exploration of the Activation Mechanism of the Epigenetic Regulator MLL3: A QM/MM Study

2021

The mixed lineage leukemia 3 or MLL3 is the enzyme in charge of the writing of an epigenetic mark through the methylation of lysine 4 from the N-terminal domain of histone 3 and its deregulation has been related to several cancer lines. An interesting feature of this enzyme comes from its regulation mechanism, which involves its binding to an activating dimer before it can be catalytically functional. Once the trimer is formed, the reaction mechanism proceeds through the deprotonation of the lysine followed by the methyl-transfer reaction. Here we present a detailed exploration of the activation mechanism through a QM/MM approach focusing on both steps of the reaction, aiming to provide new…

570StereochemistryLysineTrimerMolecular Dynamics Simulation01 natural sciencesBiochemistryMicrobiologyenzyme catalysisDFTArticleEpigenesis GeneticEnzyme catalysisQM/MM03 medical and health sciencesResidue (chemistry)Deprotonation0103 physical sciencesprotein regulationHumanscancerCàncerMolecular Biology030304 developmental biology0303 health sciencesBinding Sites010304 chemical physicsbiologyChemistryLysineNuclear ProteinsMethylation540QR1-502DNA-Binding ProteinsHistonebiology.proteinTyrosinemethyltransferaseProtein MultimerizationProtonsProteïnesTranscription Factors
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Protonation of the Biliverdin IXα Chromophore in the Red and Far-Red Photoactive States of a Bacteriophytochrome

2019

The tetrapyrrole chromophore biliverdin IXα (BV) in the bacteriophytochrome from Deinococcus radiodurans (DrBphP) is usually assumed to be fully protonated, but this assumption has not been systematically validated by experiments or extensive computations. Here, we use force field molecular dynamics simulations and quantum mechanics/molecular mechanics calculations with density functional theory and XMCQDPT2 methods to investigate the effect of the five most probable protonation forms of BV on structural stability, binding pocket interactions, and absorption spectra in the two photochromic states of DrBphP. While agreement with X-ray structural data and measured UV/vis spectra suggest that …

Absorption spectroscopyProtein ConformationPopulationProtonationMolecular Dynamics SimulationCrystallography X-Ray010402 general chemistryPhotochemistry01 natural sciencesArticlequantum chemistrychemistry.chemical_compoundMolecular dynamicsPhotochromismBacterial Proteins0103 physical scienceskvanttikemiaMaterials ChemistrymolekyylidynamiikkaPhysical and Theoretical Chemistryeducationta116excited statesphytochromeeducation.field_of_studyBinding SitesBiliverdin010304 chemical physicsChemistryBiliverdineta1182Chromophoremolecular dynamics3. Good health0104 chemical sciencesSurfaces Coatings and FilmsSpectrophotometry UltravioletDensity functional theoryDeinococcusvalokemiaproteiinitThe Journal of Physical Chemistry B
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Exploring kainate receptor pharmacology using molecular dynamics simulations.

2010

Ionotropic glutamate receptors (iGluRs) are enticing targets for pharmaceutical research; however, the search for selective ligands is a laborious experimental process. Here we introduce a purely computational procedure as an approach to evaluate ligand–iGluR pharmacology. The ligands are docked into the closed ligand-binding domain and during the molecular dynamics (MD) simulation the bi-lobed interface either opens (partial agonist/antagonist) or stays closed (agonist) according to the properties of the ligand. The procedure is tested with closely related set of analogs of the marine toxin dysiherbaine bound to GluK1 kainate receptor. The modeling is set against the abundant binding data …

AgonistModels Molecularmedicine.drug_classProtein ConformationIn silicoKainate receptorPharmacologyMolecular Dynamics SimulationLigandsPartial agonistArticleTurn (biochemistry)Cellular and Molecular NeuroscienceStructure-Activity RelationshipReceptors Kainic AcidmedicineStructure–activity relationshipPharmacologyAlanineMolecular StructureChemistryBridged Bicyclo Compounds HeterocyclicIonotropic glutamate receptorMarine ToxinsMarine toxinProtein BindingNeuropharmacology
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Structural Mechanism of N-Methyl-D-Aspartate Receptor Type 1 Partial Agonism

2012

N-methyl-D-aspartate (NMDA) receptors belong to a family of ionotropic glutamate receptors that contribute to the signal transmission in the central nervous system. NMDA receptors are heterotetramers that usually consist of two GluN1 and GluN2 monomers. The extracellular ligand-binding domain (LBD) of a monomer is comprised of discontinuous segments that form the functional domains D1 and D2. While the binding of a full agonist glycine to LBD of GluN1 is linked to cleft closure and subsequent ion-channel opening, partial agonists are known to activate the receptor only sub-maximally. Although the crystal structures of the LBD of related GluA2 receptor explain the mechanism for the partial a…

AgonistProtein Structuremedicine.drug_classGlycineMolecular ConformationBiophysicslcsh:MedicineMolecular Dynamics SimulationLigandsta3111Receptors N-Methyl-D-AspartateBiochemistryBiophysics Simulationsta3112Partial agonistIon ChannelsChemical BiologyMacromolecular Structure AnalysismedicineBiomacromolecule-Ligand Interactionslcsh:ScienceReceptorBiologyta116Ion channelCrystallographyMultidisciplinaryChemistrylcsh:Rta1182Glutamate receptorProteinsComputational BiologyNeurotransmittersProtein Structure TertiaryTransmembrane ProteinsBiochemistryCycloserineBiophysicsNMDA receptorLigand-gated ion channellcsh:Qhormones hormone substitutes and hormone antagonistsProtein BindingResearch ArticleNeuroscienceIonotropic effectPLoS ONE
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Liquid structure of a water-in-salt electrolyte with a remarkably asymmetric anion

2021

Water-in-salt systems, i.e., super-concentrated aqueous electrolytes, such as lithium bis(trifluoromethanesulfonyl)imide (21 mol/kgwater), have been recently discovered to exhibit unexpectedly large electrochemical windows and high lithium transference numbers, thus paving the way to safe and sustainable charge storage devices. The peculiar transport features in these electrolytes are influenced by their intrinsically nanoseparated morphology, stemming from the anion hydrophobic nature and manifesting as nanosegregation between anions and water domains. The underlying mechanism behind this structure-dynamics correlation is, however, still a matter of strong debate. Here, we enhance the apol…

AnionsDYNAMICSLI+MOLECULAR-FORCE FIELDLOCAL-STRUCTUREWaterLithiumMolecular Dynamics Simulationmolecular-force field; particle meshewald; local-structure; ionic liquids; dynamics; viscosity; conductivity dependence; LI+PARTICLE MESH EWALElectrolytesIONIC LIQUIDSDEPENDENCECONDUCTIVITYVISCOSITY
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Recent advances in computational design of potent aromatase inhibitors: open-eye on endocrine-resistant breast cancers.

2019

Introduction: The vast majority of breast cancers (BC) are estrogen receptor positive (ER+). The most effective treatments to fight this BC type rely on estrogen deprivation therapy, by inhibiting the aromatase enzyme, which performs estrogen biosynthesis, or on blocking the estrogens signaling path via modulating/degrading the estrogen's specific nuclear receptor (estrogen receptor-?, ER?). While being effective at early disease stage, patients treated with aromatase inhibitors (AIs) may acquire resistance and often relapse after prolonged therapies. Areas covered: In this compendium, after an overview of the historical development of the AIs currently in clinical use, and of the computati…

Antineoplastic Agents Hormonalmedicine.drug_classCYP450sEstrogen receptorallostery; aromatase inhibitors; Breast cancer; CYP450s; ligand-based and structure-based drug design; molecular dynamics; virtual screeningBreast NeoplasmsMolecular Dynamics SimulationBioinformatics03 medical and health sciencesBreast cancer0302 clinical medicineBreast cancerDrug DiscoverymedicineEndocrine systemHumansAromataseSurvival rate030304 developmental biologyCause of deathNeoplasm Staging0303 health sciencesallosterybiologybusiness.industryAromatase Inhibitorsvirtual screeningmedicine.diseaseligand-based and structure-based drug designmolecular dynamicsSurvival RateNuclear receptorEstrogenDrug Resistance Neoplasm030220 oncology & carcinogenesisDrug Designbiology.proteinFemalebusinessExpert opinion on drug discovery
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