Search results for "Quantitative"

showing 10 items of 2409 documents

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
researchProduct

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
researchProduct

Orientational landscapes of peptides in membranes: prediction of (2)H NMR couplings in a dynamic context.

2009

Unlike soluble proteins, membrane polypeptides face an anisotropic milieu. This imposes restraints on their orientation and provides a reference that makes structure prediction tractable by minimalistic thermodynamic models. Here we use this framework to build orientational distributions of monomeric membrane-bound peptides and to predict their expected solid-state (2)H NMR quadrupolar couplings when labeled at specific side chain positions. Using a complete rigid-body sampling of configurations relative to an implicit lipid membrane, peptide free energy landscapes are calculated. This allows us to obtain probability distributions of the peptide tilt, azimuthal rotation, and depth of membra…

Models MolecularMagnetic Resonance SpectroscopyMembrane FluidityPopulationDegrees of freedom (physics and chemistry)Context (language use)BiochemistryQuantitative Biology::Subcellular ProcessesComputational chemistryOrientation (geometry)Computer SimulationLipid bilayereducationAnisotropyPhysics::Biological PhysicsQuantitative Biology::Biomoleculeseducation.field_of_studyChemistryCell MembraneMaxima and minimaMembraneSolubilityChemical physicsThermodynamicsPeptidesAlgorithmsBiochemistry
researchProduct

Ion transport and selectivity in nanopores with spatially inhomogeneous fixed charge distributions

2007

Polymeric nanopores with fixed charges show ionic selectivity when immersed in aqueous electrolyte solutions. The understanding of the electrical interaction between these charges and the mobile ions confined in the inside nanopore solution is the key issue in the design of potential applications. The authors have theoretically described the effects that spatially inhomogeneous fixed charge distributions exert on the ionic transport and selectivity properties of the nanopore. A comprehensive set of one-dimensional distributions including the skin, core, cluster, and asymmetric cases are analyzed on the basis of the Nernst-Planck equations. Current-voltage curves, nanopore potentials, and tr…

Models MolecularMaterials scienceStatic ElectricityGeneral Physics and AstronomyIonic bondingNanotechnologyElectrolyteIon ChannelsNanoporous materialsIonQuantitative Biology::Subcellular ProcessesElectrolytesBiopolymersIonic conductivityStatic electricityCluster (physics)Ionic conductivityComputer SimulationPhysical and Theoretical Chemistry:FÍSICA::Química física [UNESCO]AnisotropyIon TransportUNESCO::FÍSICA::Química físicaNanostructuresNanoporeModels ChemicalPolymer solutionsChemical physicsNanoporous materials ; Polymer solutions ; Electrolytes ; Ionic conductivityAnisotropyIon Channel GatingPorosityThe Journal of Chemical Physics
researchProduct

Atomic Mean-Square Displacements in Proteins by Molecular Dynamics: A Case for Analysis of Variance

2004

AbstractInformation on protein internal motions is usually obtained through the analysis of atomic mean-square displacements, which are a measure of variability of the atomic positions distribution functions. We report a statistical approach to analyze molecular dynamics data on these displacements that is based on probability distribution functions. Using a technique inspired by the analysis of variance, we compute unbiased, reliable mean-square displacements of the atoms and analyze them statistically. We applied this procedure to characterize protein thermostability by comparing the results for a thermophilic enzyme and a mesophilic homolog. In agreement with previous experimental observ…

Models MolecularMean squareSurface (mathematics)Hot TemperatureTime FactorsNitrogenProtein ConformationMolecular ConformationBiophysicsBiophysical Theory and ModelingMeasure (mathematics)Protein Structure SecondaryMolecular dynamicsBacterial ProteinsStatistical physicsProbabilityThermostabilityAnalysis of VarianceQuantitative Biology::BiomoleculesModels StatisticalChemistryProteinsModels TheoreticalCrystallographyDistribution functionSolventsProbability distributionAnalysis of varianceAlgorithms
researchProduct

Field theoretic study of bilayer membrane fusion: I. Hemifusion mechanism

2003

Self-consistent field theory is used to determine structural and energetic properties of metastable intermediates and unstable transition states involved in the standard stalk mechanism of bilayer membrane fusion. A microscopic model of flexible amphiphilic chains dissolved in hydrophilic solvent is employed to describe these self-assembled structures. We find that the barrier to formation of the initial stalk is much smaller than previously estimated by phenomenological theories. Therefore its creation it is not the rate limiting process. The barrier which is relevant is associated with the rather limited radial expansion of the stalk into a hemifusion diaphragm. It is strongly affected by…

Models MolecularMembrane FluidityLipid BilayersStatic ElectricityBiophysicsFOS: Physical sciencesCondensed Matter - Soft Condensed Matter010402 general chemistryCurvatureQuantitative Biology - Quantitative MethodsMembrane Fusion01 natural sciencesQuantitative Biology::Subcellular Processes03 medical and health sciencesElectromagnetic FieldsMetastabilityPhase (matter)Computer SimulationLipid bilayerQuantitative Methods (q-bio.QM)030304 developmental biology0303 health sciencesFusionMembranesChemistryBilayerLipid bilayer fusionMembranes Artificial0104 chemical sciencesCrystallographyMembraneModels ChemicalChemical physicsFOS: Biological sciencesSoft Condensed Matter (cond-mat.soft)Porosity
researchProduct

Molecular Rearrangement of an Aza-Scorpiand Macrocycle Induced by pH: A Computational Study †

2016

Rearrangements and their control are a hot topic in supramolecular chemistry due to the possibilities that these phenomena open in the design of synthetic receptors and molecular machines. Macrocycle aza-scorpiands constitute an interesting system that can reorganize their spatial structure depending on pH variations or the presence of metal cations. In this study, the relative stabilities of these conformations were predicted computationally by semi-empirical and density functional theory approximations, and the reorganization from closed to open conformations was simulated by using the Monte Carlo multiple minimum method Financial support by the Spanish Ministerio de Economía y Competitiv…

Models MolecularMontecarlo Mètode deMonte Carlo method01 natural sciencessupramolecular chemistryMonte Carlo Multiple Minimumlcsh:ChemistryComputational chemistryaza-scorpiandsMolecular rearrangementpH controlled; supramolecular chemistry; synthetic receptors; aza-scorpiands; semi-empirical; Density Functional Theory; Monte Carlo Multiple Minimumlcsh:QH301-705.5semi-empiricalSpectroscopyDensity Functional TheoryDensity functionalsSpatial structureChemistryGeneral MedicineHydrogen-Ion ConcentrationMolecular machineComputer Science ApplicationsMonte Carlo methodpH controlledvisual_artsynthetic receptorsvisual_art.visual_art_mediumDensity functional theoryMonte Carlo MethodMacrocyclic CompoundsSupramolecular chemistry010402 general chemistryQuímica supramolecularCatalysisArticleInorganic ChemistryMetalQuantitative Biology::Subcellular ProcessesPhysical and Theoretical ChemistryMolecular BiologyAza CompoundsFuncional de densitat Teoria del010405 organic chemistryOrganic ChemistryComputational Biology0104 chemical scienceslcsh:Biology (General)lcsh:QD1-999Synthetic ReceptorsQuantum TheorySupramolecular chemistryInternational Journal of Molecular Sciences
researchProduct

How molecular knots can pass through each other

2014

We propose a mechanism in which two molecular knots pass through each other and swap positions along a polymer strand. Associated free energy barriers in our simulations only amount to a few $k_{B}T$, which may enable the interchange of knots on a single DNA strand.

Models MolecularMultidisciplinaryComputersPolymersChemistryFOS: Physical sciencesBiomolecules (q-bio.BM)DNACondensed Matter - Soft Condensed MatterMolecular physicsNanostructuresDiffusionMolecular dynamicsCrystallographyQuantitative Biology - BiomoleculesBiological Physics (physics.bio-ph)FOS: Biological sciencesPhysical SciencesNucleic Acid ConformationThermodynamicsSoft Condensed Matter (cond-mat.soft)Physics - Biological Physics
researchProduct

DesMol2, an Effective Tool for the Construction of Molecular Libraries and Its Application to QSAR Using Molecular Topology

2019

A web application, DesMol2, which offers two main functionalities, is presented: the construction of molecular libraries and the calculation of topological indices. These functionalities are explained through a practical example of research of active molecules to the formylpeptide receptor (FPR), a receptor associated with chronic inflammation in systemic amyloidosis and Alzheimer&rsquo

Models MolecularMultilinear mapQuantitative structure–activity relationshiplinear discriminant analysisComputer scienceQuantitative Structure-Activity RelationshipPharmaceutical ScienceComputational biology01 natural sciencesArticleAnalytical ChemistrySmall Molecule Librarieslcsh:QD241-44103 medical and health scienceslcsh:Organic chemistryDrug DiscoveryPhysical and Theoretical ChemistryPiperazineDesMol2030304 developmental biology0303 health sciencesMolecular Structure010405 organic chemistryOrganic Chemistrymolecular librariesBase (topology)Linear discriminant analysisReceptors Formyl PeptideSystemic amyloidosis0104 chemical sciencestopology descriptorsmultilinear regression analysisDiscriminantChemistry (miscellaneous)Molecular MedicineMultiple linear regression analysisMolecular topologyAlzheimer’s diseaseDatabases ChemicalSoftwareProtein BindingMolecules
researchProduct

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
researchProduct