Search results for "molecular dynamics"

showing 10 items of 1075 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
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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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Hydrogen bonding in dimers of tritolyl and tritosylurea derivatives of triphenylmethanes.

2006

The crystal structure of the homodimer formed by the tritolylurea 3a proves the existence of a belt of six bifurcated hydrogen bonds between both NH and the O=C groups of the adjacent urea residues. For the tritosylurea 3b, four additional three-center hydrogen bonds, also involving the SO2 oxygen, are found in the crystalline state. Molecular dynamics simulations in a chloroform box confirm these patterns of the hydrogen bonds and the resulting elongation of the dimer 3b. 3b in comparison to 3a x 3a. The calculated complexation energies for the three dimeric combinations are nearly identical in agreement with the simultaneous formation of heterodimer 3a x 3b in a mixture of 3a and 3b.

Models MolecularMagnetic Resonance SpectroscopyDimerLow-barrier hydrogen bondMolecular Conformationchemistry.chemical_elementCrystal structurePhotochemistryCrystallography X-RayBiochemistryOxygenchemistry.chemical_compoundMolecular dynamicsUreaComputer SimulationPhysical and Theoretical ChemistryChloroformHydrogen bondOrganic ChemistryHydrogen BondingTrityl CompoundsCrystallographychemistryUreaThermodynamicsDimerizationOrganicbiomolecular chemistry
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Antimicrobial Peptides and Their Superior Fluorinated Analogues: Structure-Activity Relationships as Revealed by NMR Spectroscopy and MD Calculations

2010

9 pag., 6 fig, 3 tab.

Models MolecularMagnetic Resonance SpectroscopyHalogenationProtein ConformationDiffusionAntimicrobial peptidesMicrobial Sensitivity TestsMolecular Dynamics SimulationBiochemistryMicelleStructure-Activity RelationshipMolecular dynamicsantimicrobial peptidesNMR spectroscopyComputational chemistryfluorineEscherichia coliOrganic chemistryAmino Acid SequenceMolecular BiologyAqueous solutionMolecular StructureChemistryOrganic ChemistrySodium Dodecyl SulfateWaterNuclear magnetic resonance spectroscopyAntimicrobialmolecular dynamicsSolutionsMembranemembranespeptidesMolecular MedicineAntimicrobialSDS micellesOligopeptidesAntimicrobial Cationic Peptides
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Conformational and structural analysis of the equilibrium between single- and double-strand ?-helix of aD,L-alternating oligonorleucine

2004

Alternating sequences of D and L residues in peptides are directly related to the formation of several kinds of regular helical conformations usually called beta-helices. The major feature of these structures is that they can be associated with the transmembrane ion-conducting channel activity in some natural antibacterial peptides. The study of alternating D,L synthetic peptides is critical to understand how factors such as surrounding media, main chain length, type of side chain and terminal groups, among others, can determine the adoption of a specific kind of beta-helix. Early studies pointed out that the peptides Boc-(D-NLeu-L-NLeu)(6)-D-MeNLe-L-Nl-D-Nl-L-Nl-OMe (Boc: tert-butyloxycarb…

Models MolecularMagnetic Resonance SpectroscopyProtein ConformationStereochemistryDimerMolecular Sequence DataBiophysicsDNA Single-StrandedBeta helixStereoisomerismAntiparallel (biochemistry)BiochemistryProtein Structure SecondaryBiomaterialsMolecular dynamicschemistry.chemical_compoundProtein structureNorleucineSide chainAmino Acid SequenceChemistryOrganic ChemistryStereoisomerismDNAGeneral MedicineNuclear magnetic resonance spectroscopyCrystallographyNucleic Acid ConformationThermodynamicsOligopeptidesBiopolymers
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Orientational preferences of aromatic guests in dimeric capsules of tetraurea calix[4]arenes—MD and NMR studies

2006

Molecular dynamics (MD) simulations have been performed for complexes of a dimeric capsule of a tetraurea calixarene with a series of twelve aromatic guests. A distinct orientational preference and a restriction of the internal mobility was found which depend on the size and electronic properties of the guests. The results are in agreement with the CIS values obtained from (1)H NMR spectroscopic measurements and with complexation selectivities obtained by competition experiments.

Models MolecularMagnetic Resonance SpectroscopyPyridinesChemistryOrganic ChemistryBinding CompetitiveBiochemistrySubstrate SpecificityKineticsMolecular dynamicsCrystallographyPhenolsPyrazinesCalixareneBenzene DerivativesProton NMRThermodynamicsUreaCalixarenesPhysical and Theoretical ChemistryElectronic propertiesOrg. Biomol. Chem.
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Dynamic and electronic transport properties of DNA translocation through graphene nanopores

2013

Graphene layers have been targeted in the last years as excellent host materials for sensing a remarkable variety of gases and molecules. Such sensing abilities can also benefit other important scientific fields such as medicine and biology. This has automatically led scientists to probe graphene as a potential platform for sequencing DNA strands. In this work, we use robust numerical tools to model the dynamic and electronic properties of molecular sensor devices composed of a graphene nanopore through which DNA molecules are driven by external electric fields. We performed molecular dynamic simulations to determine the relation between the intensity of the electric field and the transloca…

Models MolecularMaterials scienceBioengineeringNanotechnologyMolecular Dynamics Simulationlaw.inventionElectron Transportsymbols.namesakeMolecular dynamicsNanoporeslawElectric fieldGeneral Materials Scienceta114GrapheneMechanical EngineeringFermi levelMolecular sensorMolecular electronicsGeneral ChemistryDNACondensed Matter PhysicsNanoporesymbolsGraphiteBiosensorNano Letters
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