Search results for "X-Ray scattering"

showing 10 items of 165 documents

Small-angle X-ray Scattering-based Three-dimensional Reconstruction of the Immunogen KLH1 Reveals Different Oxygen-dependent Conformations

2003

For decades the respiratory protein keyhole limpet hemocyanin (KLH1) from the marine gastropod Megathura crenulata has been used widely as a potent immunostimulant, useful hapten carrier, and valuable agent in the treatment of bladder carcinoma. Although much information on the immunological properties of KLH1 is available, biochemical and structural data are still incomplete. Small-angle x-ray scattering revealed the existence of two conformations, an oxy state being slightly more compact than the deoxy state. Based on small-angle scattering curves, a newly developed Monte Carlo algorithm delivered a surface representation of proteins. The massive changes of the surfaces of reconstructed d…

Models MolecularProtein Conformationmedicine.medical_treatmentMegathura crenulataCrystallography X-RayBiochemistryAllosteric RegulationmedicineAnimalsScattering RadiationMoleculeAntigensMolecular BiologybiologyScatteringSmall-angle X-ray scatteringHemocyaninCell Biologybiology.organism_classificationOxygenRespiratory proteinMicroscopy ElectronCrystallographyMolluscaHemocyaninsbiology.proteinHaptenKeyhole limpet hemocyaninJournal of Biological Chemistry
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Crystal Structure of Human Filamin C Domain 23 and Small Angle Scattering Model for Filamin C 23–24 Dimer

2007

Filamin C is a dimeric, actin-binding protein involved in organization of cortical cytoskeleton and of the sarcomere. We performed crystallographic, small-angle X-ray scattering and analytical ultracentrifugation experiments on the constructs containing carboxy-terminal domains of the protein (domains 23-24 and 19-21). The crystal structure of domain 23 of filamin C showed that the protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray scattering experiments performed on filamin C tandem Ig-like domains 23 and 24 reveal a dimer that is formed by domain 24 and that domain 23 has little interactions with itself or with domain 24, while the analytical ultracentrifugation …

Models MolecularProtein FoldingFilaminsDimermacromolecular substancesCrystal structureCrystallography X-RayFilaminSarcomereAnalytical Ultracentrifugationchemistry.chemical_compoundContractile ProteinsNickelStructural BiologyScattering Small AngleHumansMolecular BiologyBinding SitesSmall-angle X-ray scatteringScatteringMicrofilament ProteinsProtein Structure TertiaryCrystallographychemistrySmall-angle scatteringDimerizationUltracentrifugationJournal of Molecular Biology
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Small-angle X-ray scattering reveals compact domain-domain interactions in the N-terminal region of filamin C

2014

Filamins are multi-domain, actin cross-linking, and scaffolding proteins. In addition to the actin cross-linking function, filamins have a role in mechanosensor signaling. The mechanosensor function is mediated by domain-domain interaction in the C-terminal region of filamins. Recently, we have shown that there is a three-domain interaction module in the Nterminal region of filamins, where the neighboring domains stabilize the structure of the middle domain and thereby regulate its interaction with ligands. In this study, we have used small-angle X-ray scattering as a tool to screen for potential domain-domain interactions in the N-terminal region. We found evidence of four domain-domain in…

Models MolecularScaffold proteinProtein StructureProtein ConformationFilaminslcsh:Medicinemacromolecular substancesBiologyFilaminBiochemistryProtein–protein interactionProtein structureX-Ray Diffractioncompact domain-domain interactionsScattering Small AngleMacromolecular Structure AnalysisProtein InteractionsCytoskeletonlcsh:ScienceMolecular BiologyActinMultidisciplinarySmall-angle X-ray scatteringlcsh:Rta1182Biology and Life SciencesProteinsComputational BiologyRecombinant ProteinsProtein Structure TertiaryCell biologyCytoskeletal Proteinssmall-angle X-ray scatteringDomain (ring theory)Biophysicslcsh:QGlobular ProteinsStructural ProteinsResearch Articlefilamin CPloS One
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Glutamate 270 plays an essential role in K+-activation and domain closure ofThermus thermophilusisopropylmalate dehydrogenase

2014

The mutant E270A of Thermus thermophilus 3-isopropylmalate dehydrogenase exhibits largely reduced (∼1%) catalytic activity and negligible activation by K(+) compared to the wild-type enzyme. A 3-4 kcal/mol increase in the activation energy of the catalysed reaction upon this mutation could also be predicted by QM/MM calculations. In the X-ray structure of the E270A mutant a water molecule was observed to take the place of K(+). SAXS and FRET experiments revealed the essential role of E270 in stabilisation of the active domain-closed conformation of the enzyme. In addition, E270 seems to position K(+) into close proximity of the nicotinamide ring of NAD(+) and the electron-withdrawing effect…

Models MolecularStereochemistry030303 biophysicsMutantBiophysicsGlutamic AcidLarge scale facilities for research with photons neutrons and ionsSmall angle X-ray scatteringDehydrogenaseBiochemistry3-Isopropylmalate Dehydrogenase03 medical and health scienceschemistry.chemical_compoundIsopropylmalate dehydrogenaseFluorescence resonance energy transferStructural BiologyOxidoreductaseGeneticsMolecular BiologyX-ray crystallography030304 developmental biologychemistry.chemical_classificationSite-directed mutagenesis0303 health sciencesNicotinamidebiologyThermus thermophilusActivation by K+Cell BiologyThermus thermophilusbiology.organism_classificationProtein Structure TertiaryMOPSEnzyme ActivationKineticsCrystallographyEnzymechemistryMutationNAD+ kinaseFEBS Letters
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The C-terminal rod 2 fragment of filamin A forms a compact structure that can be extended

2012

Filamins are large proteins that cross-link actin filaments and connect to other cellular components. The C-terminal rod 2 region of FLNa (filamin A) mediates dimerization and interacts with several transmembrane receptors and intracellular signalling adaptors. SAXS (small-angle X-ray scattering) experiments were used to make a model of a six immunoglobulin-like domain fragment of the FLNa rod 2 (domains 16–21). This fragment had a surprising three-branched structural arrangement, where each branch was made of a tightly packed two-domain pair. Peptides derived from transmembrane receptors and intracellular signalling proteins induced a more open structure of the six domain fragment. Mutagen…

Models Moleculargenetics [Receptors Dopamine D3]metabolism [Recombinant Proteins]Protein Conformationgenetics [Antigens CD18]chemistry [Recombinant Proteins]Plasma protein bindingCrystallography X-RayLigandsFilaminmetabolism [Antigens CD18]metabolism [Cytoskeletal Proteins]BiochemistryfilaminsContractile ProteinsProtein structuremetabolism [Peptide Fragments]FLNAchemistry [Antigens CD18]genetics [Cell Adhesion Molecules]Small-angle X-ray scatteringMicrofilament Proteinsgenetics [Contractile Proteins]Recombinant Proteinschemistry [Receptors Dopamine D3]FBLIM1 protein humanddc:540Domain (ring theory)DimerizationProtein Bindingchemistry [Contractile Proteins]FilaminsAntigens CD18metabolism [Cell Adhesion Molecules]BiologyScattering Small Anglemetabolism [Receptors Dopamine D3]Humanschemistry [Microfilament Proteins]Protein Interaction Domains and Motifsmetabolism [Mutant Proteins]DRD3 protein humanMolecular Biologymetabolism [Contractile Proteins]Actingenetics [Cytoskeletal Proteins]Cryoelectron MicroscopyMutagenesista1182Receptors Dopamine D3metabolism [Microfilament Proteins]Cell Biologychemistry [Cell Adhesion Molecules]genetics [Peptide Fragments]Peptide FragmentsCytoskeletal ProteinsCrystallographychemistry [Mutant Proteins]chemistry [Peptide Fragments]CD18 AntigensBiophysicschemistry [Cytoskeletal Proteins]Mutant Proteinsgenetics [Microfilament Proteins]Cell Adhesion MoleculesBiochemical Journal
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On the nature of morphological features in phase-separated (PEO)nNaSCN mixtures: a SAXS investigation

2000

Abstract The SAXS technique is used to throw light on the morphology of phase-separated poly(ethylene oxide)n–sodium thiocyanate [(PEO)nNaSCN] mixtures. A temperature-dependent investigation is reported for (PEO)4.5NaSCN. (PEO)nNaSCN mixtures show a complex phase behaviour. At the investigated composition, a crystalline complex (CC) is formed between PEO and NaSCN. The considered composition is representative of thermodynamic states where three different phases coexist simultaneously: crystalline PEO (CPEO), amorphous PEO (APEO) and crystalline complex (CC). Various SAXS data analysis approaches are presented to understand the nature of these coexisting phases. Invariant analysis shows a bi…

Morphology (linguistics)Ethylene oxideChemistrySmall-angle X-ray scatteringGeneral ChemistryCondensed Matter PhysicsAmorphous solidchemistry.chemical_compoundCorrelation functionChemical engineeringPhase (matter)Polymer chemistryGeneral Materials ScienceLamellar structureSodium thiocyanateSolid State Ionics
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Mild Homogeneous Synthesis of Gold Nanoparticles through the Epoxide Route: Kinetics, Mechanisms, and Related One‐Pot Composites

2019

A new one-pot homogeneous methodology at room temperature to obtain Au nanoparticles (AuNP) on the basis of the epoxide route is presented. The proposed method takes advantage of the homogenous generation of OH- moieties driven by epoxide ring-opening, mediated by chloride nucleophilic attack. Once reached alkaline conditions, the reducing medium allows the quantitative formation of AuNP under well-defined kinetic control. A stabilizing agent, such as polyvinylpyrrolidone (PVP) or cetyltrimethylammonium chloride (CTAC), is required to maintain the AuNP stable. Meanwhile their presence dramatically affects the reduction kinetics and pathway, as demonstrated by the evolution of the UV/Vis spe…

NanocompositePolyvinylpyrrolidone010405 organic chemistrySmall-angle X-ray scatteringOrganic ChemistryKineticsEpoxideNanoparticleGeneral Chemistry010402 general chemistry01 natural sciencesChlorideCatalysis0104 chemical scienceschemistry.chemical_compoundchemistryChemical engineeringColloidal goldmedicinemedicine.drugChemistry – A European Journal
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On the Role of Extensional Flow in Morphology and Property Modifications of MWCNT/Polyamide-Based Fibers

2011

Unfilled and MWCNT-filled PA fibers are prepared and the effect of the extensional flow on their mechanical performance and morphological variations is investigated. Morphological analyses using SEM, TEM, and SAXS suggest a stronger orientation of the MWCNTs along the fiber direction with increasing extensional flow. A particular MWCNT bundle formation in the PA drawn nanocomposite fibers is observed for the first time, and a pull-out of the central nanotube in some bundles is noted. The maintenance of the "shish-kebab" structure upon extensional flow is responsible for the mechanical improvements and dimensional stability in MWCNT-filled PA fibers.

NanotubeNanocompositeMaterials scienceMorphology (linguistics)Polymers and PlasticsSmall-angle X-ray scatteringGeneral Chemical EngineeringOrganic ChemistryCarbon nanotubelaw.inventionSynthetic fiberlawPolyamideMaterials ChemistryFiberComposite materialMacromolecular Materials and Engineering
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Combination of acoustic levitation with small angle scattering techniques and synchrotron radiation circular dichroism. Application to the study of p…

2016

Abstract Background The acoustic levitation technique is a useful sample handling method for small solid and liquids samples, suspended in air by means of an ultrasonic field. This method was previously used at synchrotron sources for studying pharmaceutical liquids and protein solutions using x-ray diffraction and small angle x-ray scattering (SAXS). Methods In this work we combined for the first time this containerless method with small angle neutron scattering (SANS) and synchrotron radiation circular dichroism (SRCD) to study the structural behavior of proteins in solutions during the water evaporation. SANS results are also compared with SAXS experiments. Results The aggregation behavi…

Neutron diffractionBiophysicsEvaporationAnalytical chemistry02 engineering and technology010402 general chemistryAcoustic levitation01 natural sciencesBiochemistrylaw.inventionlawScattering Small AngleAnimalsHorsesMolecular BiologyComputingMilieux_MISCELLANEOUSMyoglobinScatteringChemistrySmall-angle X-ray scatteringCircular DichroismSpectrum AnalysisProteinsWaterAcoustics[CHIM.MATE]Chemical Sciences/Material chemistry021001 nanoscience & nanotechnologySmall-angle neutron scatteringSynchrotron0104 chemical sciencesSolutionsNeutron DiffractionMuramidaseSmall-angle scattering0210 nano-technologyChickensSynchrotrons
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Recent developments in ultra–small angle neutron scattering techniques

1998

Abstract There is growing interest in the (nano−) scale structural analysis of condensed matter to study synthetic and biological polymers, colloids, porous materials, etc. Over the past two decades, small–angle neutron scattering (SANS), based on the availability of high fluxes of cold neutrons (wavelengths 4−20 A), has proven to be one of the most important tools for such investigations. This success is due to a fortuitous combination of several factors of cold neutrons: high bulk penetrating power, the ability to manipulate local scattering amplitudes via isotopic labeling or an appropriate choice of solvent (contrast variation), minimal radiation damage, and small absorption for most el…

Nuclear and High Energy PhysicsMaterials sciencebusiness.industryScatteringSmall-angle X-ray scatteringNeutron scatteringSmall-angle neutron scatteringAtomic and Molecular Physics and OpticsInelastic neutron scatteringOpticsNeutronBiological small-angle scatteringbusinessX-ray scattering techniquesNeutron News
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