Search results for " MOLECULAR DYNAMICS"

showing 10 items of 126 documents

Density functional study of Cu2+-phenylalanine complex under micro-solvation environment

2013

Abstract We present an atomistic study carried out using density functional calculations including structural relaxations and Car–Parrinello Molecular Dynamics (CPMD) simulations, aiming to investigate the structures of phenylalanine-copper (II) ([Phe-Cu] 2+ ) complexes and their micro-solvation processes. The structures of the [Phe-Cu] 2+ complex with up to four water molecules are optimized using the B3LYP/6-311++G** model in gas phase to identify the lowest energy structures at each degree of solvation ( n  = 0–4). It is found that the phenylalanine appears to be in the neutral form in isolated and mono-hydrated complexes, but in the zwitterionic form in other hydrated complexes (with n …

Models MolecularCar–Parrinello molecular dynamicsPhenylalanineMolecular ConformationDFTMolecular dynamicsMaterials ChemistryMicro-solvationMoleculePhysical and Theoretical ChemistryPhenylalanine-copper (II) complexStructural motifta116Spectroscopyta114LigandHydrogen bondChemistrySolvationHydrogen BondingComputer Graphics and Computer-Aided DesignCrystallographySolvation shellModels ChemicalCPMDCopperJOURNAL OF MOLECULAR GRAPHICS AND MODELLING
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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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DNA minor groove binders: an overview on molecular modeling and QSAR approaches

2007

Molecular recognition of DNA by small molecules and proteins is a fundamental problem in structural biology and drug design. Understanding of recognition in both sequence-selective and sequence neutral ways at the level of successful prediction of binding modes and site selectivity will be instrumental for improvements in the design and synthesis of new molecules as potent and selective gene-regulatory drugs. Minor groove is the target of a large number of non-covalent binding agents. DNA binding with specific sequences, mostly AT, takes place by means of a combination of directed hydrogen bonding to base pair edges, van der Waals interactions with the minor groove walls and generalized ele…

Models MolecularPharmacologyDNA minor groove binders (mGBs) in silico techniques molecular modeling ab initio methods docking molecular dynamics simulations (MDS) QSAR QSPR.Molecular modelBase pairStereochemistryChemistryIn silicoOrganic ChemistryQuantitative Structure-Activity RelationshipDNAComputational biologyBiochemistrySmall moleculechemistry.chemical_compoundMolecular recognitionPharmaceutical PreparationsStructural biologyDocking (molecular)Drug DesignDrug DiscoveryNucleic Acid ConformationMolecular MedicineDNA
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Homology models of melatonin receptors: challenges and recent advances

2013

Melatonin exerts many of its actions through the activation of two G protein-coupled receptors (GPCRs), named MT1 and MT2. So far, a number of different MT1 and MT2 receptor homology models, built either from the prototypic structure of rhodopsin or from recently solved X-ray structures of druggable GPCRs, have been proposed. These receptor models differ in the binding modes hypothesized for melatonin and melatonergic ligands, with distinct patterns of ligand-receptor interactions and putative bioactive conformations of ligands. The receptor models will be described, and they will be discussed in light of the available information from mutagenesis experiments and ligand-based pharmacophore …

Models MolecularProtein Conformationhomology modelingMolecular Sequence DataDruggabilityReviewComputational biologyLigandsBioinformaticsCatalysisInorganic Chemistrylcsh:ChemistryStructure-Activity Relationshipmelatonin receptorsAnimalsHumansAmino Acid SequenceHomology modelingmelatonin receptors; MT1; MT2; homology modeling; structure-activity relationships; docking; molecular dynamics simulationsPhysical and Theoretical ChemistryReceptorMolecular Biologylcsh:QH301-705.5SpectroscopyMelatoninG protein-coupled receptorBinding SitesSequence Homology Amino AcidbiologyReceptor Melatonin MT2Receptor Melatonin MT1MT1Organic ChemistryMT2structure-activity relationshipsGeneral Medicinemolecular dynamics simulationsComputer Science ApplicationsMelatonergiclcsh:Biology (General)lcsh:QD1-999Structural Homology ProteinDocking (molecular)RhodopsindockingMutagenesis Site-Directedbiology.proteinPharmacophore
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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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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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Rational design of allosteric modulators of the aromatase enzyme: An unprecedented therapeutic strategy to fight breast cancer.

2019

Estrogens play a key role in cellular proliferation of estrogen-receptor-positive (ER+) breast cancers (BCs). Suppression of estrogen production by competitive inhibitors of the enzyme aromatase (AIs) is currently one of the most effective therapies against ER + BC. Yet, the development of acquired resistance, after prolonged treatments with AIs, represents a clinical major concern. Serendipitous findings indicate that aromatase may be non-competitively inhibited by clinically employed drugs and/or industrial chemicals. Here, by performing in silico screening on two putative allosteric sites, molecular dynamics and free energy simulations, supported by enzymatic and cell-based assays, we id…

Molecular dynamicmedicine.drug_classIn silicoAllosteric regulationCytochromes P450; Aromatase; Molecular dynamics; Aromatase inhibitors; Docking; Breast cancer; Resistance onset; Mixed inhibition mechanismAntineoplastic AgentsBreast NeoplasmsMolecular dynamicsMolecular Dynamics SimulationDockingStructure-Activity RelationshipBreast cancerBreast cancerAromataseAllosteric RegulationCell Line TumorDrug DiscoverymedicineResistance onsetHumansMixed inhibition mechanismAromataseEnzyme InhibitorsCell ProliferationPharmacologychemistry.chemical_classificationbiologyDose-Response Relationship DrugMolecular StructureChemistryOrganic ChemistryRational designAromatase inhibitorGeneral Medicinemedicine.diseaseEnzymeAromatase inhibitorsSettore CHIM/03 - Chimica Generale E InorganicaEstrogenDocking (molecular)Drug Designbiology.proteinCancer researchDrug Screening Assays AntitumorCytochromes P450European journal of medicinal chemistry
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Quantitative Analysis of the Interactions of Metal Complexes and Amphiphilic Systems: Calorimetric, Spectroscopic and Theoretical Aspects.

2022

Metals and metal-based compounds have many implications in biological systems. They are involved in cellular functions, employed in the formation of metal-based drugs and present as pollutants in aqueous systems, with toxic effects for living organisms. Amphiphilic molecules also play important roles in the above bio-related fields as models of membranes, nanocarriers for drug delivery and bioremediating agents. Despite the interest in complex systems involving both metal species and surfactant aggregates, there is still insufficient knowledge regarding the quantitative aspects at the basis of their binding interactions, which are crucial for extensive comprehension of their behavior in sol…

Molecular dynamics simulationsSpeciationCalorimetryBiochemistryBiological membraneAmphiphilic systemsKineticsMetal complexesSpectrophotometrySettore CHIM/03 - Chimica Generale E InorganicaCoordination ComplexesMetalsSolution thermodynamicsDensity functional theory calculationsDrug deliveryIsothermal titration calorimetryThermodynamicsMolecular Biologymetal complexes; amphiphilic systems; drug delivery; biological membrane; solution thermodynamics; speciation; isothermal titration calorimetry; spectrophotometry; molecular dynamics simulations; density functional theory calculationsBiomolecules
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Different relaxations in myoglobin after photolysis

2004

To clarify the interplay of kinetic hole-burning (KHB), structural relaxation, and ligand migration in myoglobin (Mb), we measured time-resolved absorption spectra in the Soret region after photolysis of carbon monoxide Mb (MbCO) in the temperature interval 120-260 K and in the time window 350 ns to 200 ms. The spectral contributions of both photolyzed (Mb * ) and liganded Mb (MbCO) have been analyzed by taking into account homogeneous bandwidth, coupling to vibrational modes, and static conformational heterogeneity. We succeeded in separating the “time-dependent” spectral changes, and this work provides possibilities to identify the events in the process of ligand rebinding. KHB is domina…

Myoglobin Molecular Dynamics Simulation active siteAbsorption spectroscopyKineticsAnalytical chemistryThermodynamicsIn Vitro TechniquesKinetic energyLigandschemistry.chemical_compoundAnimalsMultidisciplinaryBinding SitesPhotolysisLigandMyoglobinPhotodissociationTemperatureWhalesBiological SciencesKineticsMyoglobinchemistrySpectrophotometryMolecular vibrationThermodynamicsCarbon monoxide
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