Search results for " Small Angle"

showing 10 items of 36 documents

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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Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase

2017

Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a t…

Models MolecularkinaasitentsyymitHistidine KinaseLightProtein ConformationScienceQCrystallography X-RayArticleProtein Structure SecondaryaktivointiBacterial ProteinsProtein DomainsX-Ray DiffractionphotoactivationScattering Small AngleNanotechnologysensor histidine kinasesNature Communications
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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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Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser

2014

We describe a method to measure ultrafast protein structural changes using time-resolved wide-angle X-ray scattering at an X-ray free-electron laser. We demonstrated this approach using multiphoton excitation of the Blastochloris viridis photosynthetic reaction center, observing an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein. This provides direct structural evidence for a 'protein quake': the hypothesis that proteins rapidly dissipate energy through quake-like structural motions. peerReviewed

Photosynthetic reaction centreMaterials scienceProtein ConformationPhysics::OpticsPhycobiliproteinsfrequency vibrational-modesRadiation DosageBiochemistryMolecular physicsArticlelaw.inventionProtein structureX-Ray Diffractionlawddc:570Scattering Small AngleMolecular Biologyta116Quantitative Biology::BiomoleculesScatteringLasersMolecular biophysicsFree-electron laserCell BiologyLaserstructural dynamicsEnergy TransferPicosecondBiophysicsUltrashort pulseBiotechnologyNature methods
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Myoglobin embedded in saccharide amorphous matrices: water-dependent domains evidenced by small angle X-ray scattering

2010

We report Small Angle X-ray Scattering (SAXS) measurements performed on samples of carboxy-myoglobin (MbCO) embedded in low-water trehalose glasses. Results showed that, in such samples, "low-protein" trehalose-water domains are present, surrounded by a protein-trehalose-water background; such finding is supported by Infrared Spectroscopy (FTIR) measurements. These domains, which do not appear in the absence of the protein and in analogous sucrose systems, preferentially incorporate the incoming water at the onset of rehydration, and disappear following large hydration. This observation suggests that, in organisms under anhydrobiosis, analogous domains could play a buffering role against th…

Photosynthetic reaction centreSucroseGLASS-TRANSITIONGeneral Physics and AstronomyInfrared spectroscopyRhodobacter sphaeroideschemistry.chemical_compoundRhodobacter sphaeroidesScattering Small AngleSpectroscopy Fourier Transform InfraredPHOSPHOLIPID-BILAYERREACTION CENTERSPhysical and Theoretical ChemistrySettore CHIM/02 - Chimica FisicabiologyScatteringSmall-angle X-ray scatteringMyoglobinTrehaloseWaterbiology.organism_classificationPROTEIN DYNAMICSTrehaloseMOLECULAR-DYNAMICS SIMULATIONAmorphous solidCrystallographyMyoglobinchemistryTHERMAL-DENATURATIONNEUTRON-SCATTERINGCARBOXY-MYOGLOBINEXTERNAL MATRIXTREHALOSE-COATED MBCO
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Controlled loading and release of beta-lactoglobulin in calcium-polygalacturonate hydrogels

2020

International audience; We show here how the structure of polygalacturonate (polyGalA) hydrogels cross-linked by Ca2+ cations via external gelation controls the loading and the release rate of betalactoglobulin (BLG), a globular protein. Hydrogels prepared from a polyGalA/BLG solution are found similar to those obtained from a polyGalA solution in our previous study (Maire du Poset, et al. Biomacromolecules 2019, 20(7), 2864-2872): they exhibit similar transparencies and gradients of mechanical properties and polyGalA concentration. The nominal BLG/polyGalA ratio of the mixtures is almost recovered within the whole mixed hydrogel despite such strong concentration gradients, except in the pa…

Polymers and Plastics[SDV]Life Sciences [q-bio]Beta-lactoglobulinBioengineeringLactoglobulinscalcium-polygalacturonatecomplex mixturesDiffusionBiomaterialsPolygalacturonateScattering Small AngleMaterials ChemistrystructureBeta-lactoglobulinbiologyChemistrytechnology industry and agriculturefood and beveragesglob (programming)HydrogelsproteinsCalcium polygalacturonateChemical engineeringSelf-healing hydrogelsbiology.proteinCalciumrelease rate of the loaded
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Polystyrene Sulfonate–Porphyrin Assemblies: Influence of Polyelectrolyte and Porphyrin Structure

2011

In this study, electrostatic self-assembly of different polystyrene sulfonates and a set of tetravalent cationic porphyrins is investigated. It is shown that association of linear polystyrene sulfonates of different molar masses yields finite size nanoscale assemblies that are stable in aqueous solution. Aggregates are compared to the ones of cylindrical brushes, revealing that both form assemblies in the 100 nm range with the charge ratio (molar ratio of porphyrin charges to polyelectrolyte charges) being determining, while the morphology of the resulting network-like assemblies is different for both polyelectrolyte architectures. For the smallest 8k polystyrene sulfonate, in addition, sto…

PorphyrinsLightStatic ElectricityMicroscopy Atomic ForcePorphyrin structurePolystyrene sulfonatechemistry.chemical_compoundScattering Small AnglePolymer chemistryMaterials ChemistryScattering RadiationPhysical and Theoretical ChemistryCationic polymerizationPorphyrinPolyelectrolyteNanostructuresSurfaces Coatings and FilmsQuaternary Ammonium CompoundsNeutron DiffractionZincchemistryPolystyrenesSpectrophotometry UltravioletSelf-assemblyPolystyreneCopperThe Journal of Physical Chemistry B
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Nucleation and Growth of CaCO3 Mediated by the Egg-White Protein Ovalbumin: A Time-Resolved in situ Study Using Small-Angle Neutron Scattering

2008

Mineralization of calcium carbonate in aqueous solutions starting from its initiation was studied by time-resolved small-angle neutron scattering (SANS). SANS revealed that homogeneous crystallization of CaCO 3 involves an initial formation of thin plate-shaped nuclei which subsequently reassemble to 3-dimensional particles, first of fractal and finally of compact structure. The presence of the egg-white protein ovalbumin leads to a different progression of mineralization through several stages; the first step represents amorphous CaCO 3, whereas the other phases are crystalline. The formation and dissolution of the amorphous phase is accompanied by Ca (2+)-mediated unfolding and cross-link…

Protein FoldingOvalbuminProtein ConformationChemistryNeutron diffractionNucleationWaterGeneral ChemistryNeutron scatteringBiochemistrySmall-angle neutron scatteringCatalysisCalcium Carbonatelaw.inventionAmorphous solidCalcium ChlorideNeutron DiffractionCrystallographyColloid and Surface ChemistrylawVateriteScattering Small AngleCrystallizationCrystallizationDissolutionJournal of the American Chemical Society
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SAXS Study on Myoglobin Embedded in Amorphous Saccharide Matrices

2011

We report on Small Angle X-ray Scattering (SAXS) measurements performed on samples of carboxy-myoglobin and met-myoglobin embedded in low hydrated matrices of four different saccharides (trehalose, sucrose, maltose and lactose). Results confirm the already reported occurrence of inhomogeneities, which are not peculiar of trehalose samples, but appear also in maltose and lactose, and in some cases also sucrose, being dependent on the sample hydration and on the presence of sodium dithionite. This behaviour confirms our previous interpretation about the nature of the inhomogeneities, and prompt it as a possible general behaviour for highly concentrated sugar matrices.

Small-angle X-ray scatteringMyoglobinBiophysicsAnalytical chemistrySurfaces and InterfacesGeneral ChemistryMaltoseDisaccharidesTrehaloseSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Sodium dithionitechemistry.chemical_compoundchemistryMyoglobinX-Ray Diffractionmyoglobin saccharide sugar trehalose sucrose maltose lactose bioprotection biopreservation SAXS Small-Angle X-Ray ScatteringScattering Small AngleAnimalsGeneral Materials ScienceSoft matterLactoseSugarMetmyoglobinBiotechnology
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Ionic liquid crystals based on 1,2,4-triazolium rings

2017

Ionic liquids crystals (ILCs) are a class of organic materials of great current interest. They show unique properties that can be exploited in many different fields, for example their use as solvents for extraction processes as well as electrolytes for batteries, fuel cells, dye-sensitised solar cells etc. [1-4] Moreover, in perfluorinated ILCs, the segregation of the perfluorocarbon chains promotes further self-organisation of the LC phases, adding to the materials further properties such as affinity for gases suitable for example in gas-storage. [5-7] A series of salts based on 5-(4-alkyloxyphenyl)-1,4-dimethyl-3-(perfluoroalkyl)-1,2,4-triazol-4-ium structures, differing in the length of …

Triazolium salts; Perfluorinated materials; Ionic liquid crystals Ionic liquids Liquid-crystalline ionic liquids Crystal structures Synthesis Small angle xray scattering Small angle neutron scattering gelsPerfluorinated materialSettore CHIM/06 - Chimica OrganicaTriazolium saltIonic liquid crystals Ionic liquids Liquid-crystalline ionic liquids Crystal structures Synthesis Small angle xray scattering Small angle neutron scattering gels
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