Search results for "Crystal"

showing 10 items of 22886 documents

Out-of-plane orientation of luminescent excitons in two-dimensional indium selenide.

2019

Van der Waals materials offer a wide range of atomic layers with unique properties that can be easily combined to engineer novel electronic and photonic devices. A missing ingredient of the van der Waals platform is a two-dimensional crystal with naturally occurring out-of-plane luminescent dipole orientation. Here we measure the far-field photoluminescence intensity distribution of bulk InSe and two-dimensional InSe, WSe2 and MoSe2. We demonstrate, with the support of ab-initio calculations, that layered InSe flakes sustain luminescent excitons with an intrinsic out-of-plane orientation, in contrast with the in-plane orientation of dipoles we find in two-dimensional WSe2 and MoSe2 at room-…

0301 basic medicineMaterials sciencePhotoluminescenceElectronic properties and materialsExcitonScienceGeneral Physics and Astronomychemistry.chemical_elementPhysics::Optics02 engineering and technologyTwo-dimensional materials7. Clean energyGeneral Biochemistry Genetics and Molecular BiologyArticleCrystal03 medical and health sciencessymbols.namesakeCondensed Matter::Materials SciencePhysics::Atomic and Molecular ClustersPhysics::Atomic Physicslcsh:ScienceMultidisciplinarybusiness.industryCondensed Matter::OtherQGeneral Chemistry021001 nanoscience & nanotechnologyCondensed Matter::Mesoscopic Systems and Quantum Hall EffectDipole030104 developmental biologySemiconductorchemistrysymbolsOptoelectronicslcsh:Qvan der Waals forcePhotonics0210 nano-technologybusinessIndiumNature communications
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The collagen type I segment long spacing (SLS) and fibrillar forms: Formation by ATP and sulphonated diazo dyes.

2016

The collagen type I segment long spacing (SLS) crystallite is a well-ordered rod-like molecular aggregate, ∼300nm in length, which is produced in vitro under mildly acidic conditions (pH 2.5-3.5) in the presence of 1mM ATP. The formation of the SLS crystallite amplifies the inherent linear structural features of individual collagen heterotrimers, due to the punctate linear distribution and summation of the bulkier amino acid side chains along the length of individual collagen heterotrimers. This can be correlated structurally with the 67nm D-banded collagen fibril that is found in vivo, and formed in vitro. Although first described many years ago, the range of conditions required for ATP-in…

0301 basic medicineMaterials sciencePolymersMethyl blueMuscle Fibers SkeletalGeneral Physics and AstronomyFibrilNegative StainingCollagen Type I03 medical and health scienceschemistry.chemical_compoundAdenosine TriphosphateStructural BiologyPolymer chemistryGeneral Materials ScienceColoring AgentsSirius RedEvans Bluechemistry.chemical_classification030102 biochemistry & molecular biologyFibrillogenesisCell BiologyPolyelectrolytesAmino acidCongo redMicroscopy Electron030104 developmental biologychemistryBiophysicsCrystalliteAzo CompoundsEvans BlueMicron (Oxford, England : 1993)
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Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases

2020

13 páginas, 6 figuras, 3 tablas

0301 basic medicineModels MolecularBioquímicaHistidine KinaseProtein ConformationScience030106 microbiologyPhosphataseGeneral Physics and AstronomyMicrobiologiaCrystallography X-RayModels BiologicalBiochemistryMicrobiologyGeneral Biochemistry Genetics and Molecular BiologyCatalysisArticleEnzyme catalysis03 medical and health sciencesResidue (chemistry)Protein structureBacterial ProteinsMultienzyme ComplexesHistidineThermotoga maritimaPhosphorylationlcsh:ScienceAuthor CorrectionHistidineX-ray crystallographyMultidisciplinaryEffectorChemistryEscherichia coli ProteinsQGeneral ChemistryHydrogen-Ion ConcentrationResponse regulator030104 developmental biologyBiochemistryMutationTrans-ActivatorsPhosphorylationlcsh:QBacterial Outer Membrane Proteins
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A Janus-Faced IM30 Ring Involved in Thylakoid Membrane Fusion Is Assembled from IM30 Tetramers.

2017

Summary Biogenesis and dynamics of thylakoid membranes likely involves membrane fusion events. Membrane attachment of the inner membrane-associated protein of 30 kDa (IM30) affects the structure of the lipid bilayer, finally resulting in membrane fusion. Yet, how IM30 triggers membrane fusion is largely unclear. IM30 monomers pre-assemble into stable tetrameric building blocks, which further align to form oligomeric ring structures, and differently sized IM30 rings bind to membranes. Based on a 3D reconstruction of IM30 rings, we locate the IM30 loop 2 region at the bottom of the ring and show intact membrane binding but missing fusogenic activity of loop 2 mutants. However, helix 7, which …

0301 basic medicineModels MolecularChemistryPeripheral membrane proteinLipid bilayer fusionBiological membraneMembrane FusionThylakoidsTransmembrane protein03 medical and health sciencesCrystallographyChloroplast Proteins030104 developmental biologyMembraneStructural BiologyMembrane biogenesisLiposomesBiophysicsProtein MultimerizationLipid bilayerMolecular BiologyIntegral membrane proteinProtein BindingStructure (London, England : 1993)
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High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy

2017

The analysis of the α-synuclein (aS) aggregation process, which is involved in Parkinson's disease etiopathogenesis, and of the structural feature of the resulting amyloid fibrils may shed light on the relationship between the structure of aS aggregates and their toxicity. This may be considered a paradigm of the ground work needed to tackle the molecular basis of all the protein-aggregation-related diseases. With this aim, we used chemical and physical dissociation methods to explore the structural organization of wild-type aS fibrils. High pressure (in the kbar range) and alkaline pH were used to disassemble fibrils to collect information on the hierarchic pathway by which distinct β-sh…

0301 basic medicineModels MolecularCircular dichroismAmyloidProtein FoldingProtein domainBeta sheetBiophysicsFibrilMicroscopy Atomic ForceSpectrum Analysis RamanDissociation (chemistry)03 medical and health sciences0302 clinical medicineProtein structureMicroscopy Electron TransmissionProtein DomainsSpectroscopy Fourier Transform InfraredEscherichia coliPressureChemistryCircular DichroismEnergy landscapeProteinsalpha synuclein amyloid recombinant proteinHydrogen-Ion ConcentrationRecombinant ProteinsCrystallography030104 developmental biologyMutationalpha-SynucleinProtein foldingProtein Conformation beta-StrandProtein Multimerization030217 neurology & neurosurgery
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On the (un)coupling of the chromophore, tongue interactions, and overall conformation in a bacterial phytochrome

2018

Phytochromes are photoreceptors in plants, fungi, and various microorganisms and cycle between metastable red light-absorbing (Pr) and far-red light-absorbing (Pfr) states. Their light responses are thought to follow a conserved structural mechanism that is triggered by isomerization of the chromophore. Downstream structural changes involve refolding of the so-called tongue extension of the phytochrome-specific GAF-related (PHY) domain of the photoreceptor. The tongue is connected to the chromophore by conserved DIP and PRXSF motifs and a conserved tyrosine, but the role of these residues in signal transduction is not clear. Here, we examine the tongue interactions and their interplay with …

0301 basic medicineModels MolecularCrystallography X-RayBiochemistrybakteeritProtein structurephotoconversionchromophore-binding domainTransferasestructural biologyCRYSTAL-STRUCTURETyrosineDEINOCOCCUS-RADIODURANSbiologyPhytochromeChemistryREARRANGEMENTSProtein Structure and FoldingDeinococcusmutagenesisBinding domainSignal TransductionMODULEPLANT PHYTOCHROMEPhenylalaninefotobiologia03 medical and health sciencesBacterial Proteinsprotein conformationcell signalingprotein structureBACTERIOPHYTOCHROMEMolecular BiologyX-ray crystallographysoluviestintäphytochromeAGP1BINDING DOMAINBinding Sitesta114030102 biochemistry & molecular biologyta1182Deinococcus radioduransCell BiologyChromophorebiology.organism_classificationphotoreceptor030104 developmental biologyStructural biologyFTIRBiophysicsTyrosineproteiinit3111 Biomedicineröntgenkristallografia
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Recombinant anthrax protective antigen: Observation of aggregation phenomena by TEM reveals specific effects of sterols.

2017

Abstract Negatively stained transmission electron microscope images are presented that depict the aggregation of recombinant anthrax protective antigen (rPA83 monomer and the PA63 prepore oligomer) under varying in vitro biochemical conditions. Heat treatment (50 °C) of rPA83 produced clumped fibrils, but following heating the PA63 prepore formed disordered aggregates. Freeze-thaw treatment of the PA63 prepore generated linear flexuous aggregates of the heptameric oligomers. Aqueous suspensions of cholesterol microcrystals were shown to bind small rPA83 aggregates at the edges of the planar bilayers. With PA63 a more discrete binding of the prepores to the crystalline cholesterol bilayer ed…

0301 basic medicineModels MolecularHot TemperatureBacterial ToxinsGeneral Physics and AstronomyFibrilOligomerNegative Staining03 medical and health scienceschemistry.chemical_compoundProtein AggregatesMicroscopy Electron TransmissionStructural BiologyFreezingGeneral Materials ScienceAntigens BacterialAqueous solutionChemistryBilayerCell BiologyHydrogen-Ion ConcentrationNegative stainSterolRecombinant ProteinsCrystallographySterols030104 developmental biologyMonomerCholesterolTransmission electron microscopyCrystallizationDeoxycholic AcidMicron (Oxford, England : 1993)
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rbFOX1/MBNL1 competition for CCUG RNA repeats binding contributes to myotonic dystrophy type 1/type 2 differences

2018

Myotonic dystrophy type 1 and type 2 (DM1, DM2) are caused by expansions of CTG and CCTG repeats, respectively. RNAs containing expanded CUG or CCUG repeats interfere with the metabolism of other RNAs through titration of the Muscleblind-like (MBNL) RNA binding proteins. DM2 follows a more favorable clinical course than DM1, suggesting that specific modifiers may modulate DM severity. Here, we report that the rbFOX1 RNA binding protein binds to expanded CCUG RNA repeats, but not to expanded CUG RNA repeats. Interestingly, rbFOX1 competes with MBNL1 for binding to CCUG expanded repeats and overexpression of rbFOX1 partly releases MBNL1 from sequestration within CCUG RNA foci in DM2 muscle ce…

0301 basic medicineModels MolecularProtein Conformation alpha-Helical[SDV]Life Sciences [q-bio]General Physics and AstronomyGene ExpressionRNA-binding proteinCrystallography X-Raychemistry.chemical_compoundMOLECULAR-BASISGene expressionMBNL1Myotonic DystrophyComputingMilieux_MISCELLANEOUSMultidisciplinaryCHLORIDE CHANNELQRNA-Binding ProteinsRecombinant Proteins3. Good healthCell biologyCONGENITAL HEART-DISEASEDrosophila melanogasterThermodynamicsSKELETAL-MUSCLERNA Splicing FactorsCUG REPEATSProtein BindingRNA Splicing Factorsmusculoskeletal diseasesSTEADY-STATEcongenital hereditary and neonatal diseases and abnormalitiesScienceRBFOX1BiologyMyotonic dystrophyBinding CompetitiveGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health sciencesmedicineEscherichia coliAnimalsHumansProtein Interaction Domains and MotifsBinding siteNucleotide MotifsMuscle SkeletalSPLICING REGULATOR RBFOX2MUSCLEBLIND PROTEINSBinding SitesPRE-MESSENGER-RNARNAGeneral Chemistrymedicine.diseaseDisease Models AnimalKinetics030104 developmental biologychemistryTRIPLET REPEATRNAProtein Conformation beta-Strand3111 Biomedicine
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Structure of AP205 Coat Protein Reveals Circular Permutation in ssRNA Bacteriophages.

2016

We are thankful to the MAX-lab staff for their support during our visit at the synchrotron.; International audience; AP205 is a single-stranded RNA bacteriophage that has a coat protein sequence not similar to any other known single-stranded RNA phage. Here, we report an atomic-resolution model of the AP205 virus-like particle based on a crystal structure of an unassembled coat protein dimer and a cryo-electron microscopy reconstruction of the assembled particle, together with secondary structure information from site-specific solid-state NMR data. The AP205 coat protein dimer adopts the conserved Leviviridae coat protein fold except for the N-terminal region, which forms a beta-hairpin in …

0301 basic medicineModels MolecularRNA bacteriophageViral proteinCryo-electron microscopyProtein Conformation010402 general chemistrymedicine.disease_causeCrystallography X-Ray01 natural sciencesvirus-like particleBacteriophage03 medical and health sciencesStructural Biology[CHIM.ANAL]Chemical Sciences/Analytical chemistryLeviviridaemedicineRNA VirusesBacteriophages[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Molecular BiologyProtein secondary structurebiologyCryoelectron MicroscopyRNA[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologycircular permutationRNA PhagesCircular permutation in proteinsbiology.organism_classification3. Good health0104 chemical sciencesCrystallography030104 developmental biologycoat proteinBiophysicsLeviviridaeCapsid ProteinsJournal of molecular biology
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Kinetic evidence for interaction of TMPyP4 with two different G-quadruplex conformations of human telomeric DNA

2018

Background: Stabilization of G-quadruplex helices by small ligands has attracted growing attention because they inhibit the activity of the enzyme telomerase, which is overexpressed in> 80% cancer cells. TMPyP4, one of the most studied G-quadruplex ligands, is used as a model to show that the ligands can exhibit different binding features with different conformations of a human telomeric specific sequence. Methods: UV–Vis, FRET melting Assay, Isothermal Titration Calorimetry, Time-resolved Fluorescence lifetime, T-Jump and Molecular Dynamics. Results: TMPyP4 yields two different complexes with two Tel22 telomeric conformations in the presence of Na+ or K+. T-Jump kinetic experiments show th…

0301 basic medicineModels MolecularReaction mechanismMolecular dynamicPorphyrinsFast reactionsBiophysicsStackingTel22 conformationsMolecular dynamicsBuffersCalorimetryMolecular Dynamics SimulationG-quadruplexLigandsNucleic Acid DenaturationBiochemistryDissociation (chemistry)Chemistry Physical and theoretical03 medical and health sciencesMolecular dynamicsQuímica físicaFluorescence Resonance Energy TransferHumansFast reactionMolecular BiologyTMPyP4ChemistryTel22 conformationIsothermal titration calorimetryTelomereSmall moleculeG-QuadruplexesCrystallographyKinetics030104 developmental biologyFörster resonance energy transferOligodeoxyribonucleotidesBiophysicSettore CHIM/03 - Chimica Generale E InorganicaPotassiumNucleic Acid ConformationThermodynamicsSpectrophotometry Ultraviolet
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