Search results for "Models"

showing 10 items of 8211 documents

Subunit organization of the abalone Haliotis tuberculata hemocyanin type 2 (HtH2), and the cDNA sequence encoding its functional units d, e, f, g and…

1999

We have developed a HPLC procedure to isolate the two different hemocyanin types (HtH1 and HtH2) of the European abalone Haliotis tuberculata. On the basis of limited proteolytic cleavage, two-dimensional immunoelectrophoresis, PAGE, N-terminal protein sequencing and cDNA sequencing, we have identified eight different 40-60-kDa functional units (FUs) in HtH2, termed HtH2-a to HtH2-h, and determined their linear arrangement within the elongated 400-kDa subunit. From a Haliotis cDNA library, we have isolated and sequenced a cDNA clone which encodes the five C-terminal FUs d, e, f, g and h of HtH2. As shown by multiple sequence alignments, defg of HtH2 correspond structurally to defg from Octo…

Models Molecularfood.ingredientDNA ComplementarySequence analysismedicine.medical_treatmentMolecular Sequence DataOctopodiformesMegathura crenulataBiochemistryEvolution MolecularfoodSequence Analysis ProteinComplementary DNAmedicineAnimalsHaliotisAmino Acid SequenceCloning MolecularProtein Structure QuaternaryPeptide sequenceImmunoelectrophoresisbiologySequence Homology Amino AcidcDNA libraryHelix SnailsProtein primary structureHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationPeptide FragmentsBiochemistryMolluscaHemocyaninsEuropean journal of biochemistry
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Experimental and theoretical NMR studies of interaction between phenylalanine derivative and egg yolk lecithin

2014

The interaction of phenylalanine diamide (Ac-Phe-NHMe) with egg yolk lecithin (EYL) in chloroform was studied by 1H and 13C NMR. Six complexes EYL–Ac-Phe-NHMe, stabilized by N–H···O or/and C–H···O hydrogen bonds, were optimized at M06-2X/6-31G(d,p) level. The assignment of EYL and Ac-Phe-NHMe NMR signals was supported using GIAO (gauge including atomic orbital) NMR calculations at VSXC and B3LYP level of theory combined with STO-3Gmag basis set. Results of our study indicate that the interaction of peptides with lecithin occurs mainly in the polar ‘head’ of the lecithin. Additionally, the most probable lecithin site of H-bond interaction with Ac-Phe-NHMe is the negatively charged oxygen in …

Models Molecularfood.ingredientMagnetic Resonance SpectroscopyPhenylalanineMolecular ConformationPhenylalanineLecithinDFTchemistry.chemical_compoundfoodYolkLecithinsMaterials TestingOrganic chemistryAnimalsGeneral Materials ScienceComputer Simulationhydrogen bondChloroformBinding Sitesintermolecular interactionsHydrogen bondIntermolecular forceGeneral ChemistryCarbon-13 NMREgg YolkpeptideNMR3. Good healthCrystallographylecithinchemistryModels ChemicalChickensDerivative (chemistry)Magnetic Resonance in Chemistry
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Formation of irreversibly bound annexin A1 protein domains on POPC/POPS solid supported membranes

2008

AbstractThe specific interaction of annexin A1 with phospholipid bilayers is scrutinized by means of scanning force and fluorescence microscopy, quartz crystal microbalance, ellipsometry, and modeled by dynamic Monte Carlo simulations. It was found that POPC/POPS bilayers exhibit phase separation in POPC- and POPS-enriched domains as a function of Ca2+ concentration. Annexin A1 interacts with POPC/POPS bilayers by forming irreversibly bound protein domains with monolayer thickness on POPS-enriched nanodomains, while the attachment of proteins to the POPC-enriched regions is fully reversible. A thorough kinetic analysis of the process reveals that both, the binding constant of annexin A1 at …

Models Moleculargenetic structuresLipid BilayersBiophysicsPhospholipidAnalytical chemistryPhosphatidylserines02 engineering and technologyMicroscopy Atomic ForceBiochemistryBiophysical PhenomenaMembrane Lipids03 medical and health scienceschemistry.chemical_compoundProtein structureSFMMonolayerMicropatterned membranesAnimalsHumansPOPCMonte Carlo simulationAnnexin A1030304 developmental biologyFluorescence microscopy0303 health sciencesEllipsometrytechnology industry and agricultureCell BiologyQuartz crystal microbalanceSurface Plasmon Resonance021001 nanoscience & nanotechnologyBinding constantProtein Structure TertiaryMembraneMicroscopy FluorescencechemistryQCMPhosphatidylcholinesBiophysicsCalciumlipids (amino acids peptides and proteins)Adsorption0210 nano-technologyMonte Carlo MethodProtein BindingAnnexin A1Biochimica et Biophysica Acta (BBA) - Biomembranes
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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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Complexes of Glycolic Acid with Nitrogen Isolated in Argon Matrices. II. Vibrational Overtone Excitations

2019

Structural changes of glycolic acid (GA) complex with nitrogen induced by selective overtone excitation of the &nu

Models Molecularhydrogen bondMolecular StructureNitrogentechnology industry and agriculturematrix isolationVibrationcomputational chemistryArticlevibrational spectroscopyGlycolateslcsh:QD241-441lcsh:Organic chemistrySpectroscopy Fourier Transform Infraredvibrational overtonesense organscarboxylic acidArgonskin and connective tissue diseasesMolecules
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Palladium(II)-Stabilized Pyridine-2-Diazotates: Synthesis, Structural Characterization, and Cytotoxicity Studies

2018

Well-defined diazotates are scarce. Here we report the synthesis of unprecedented homoleptic palladium(II) diazotate complexes. The palladium(II)-mediated nitrosylation of 2-aminopyridines with NaNO2 results in the formation of metal-stabilized diazotates, which were found to be cytotoxic to human ovarian cancer cells.

Models Molecularinorganic chemicalsCell SurvivalPyridinesPyrazine Diazohydroxidechemistry.chemical_elementAntineoplastic AgentsorganometalliyhdisteetCrystallography X-Ray010402 general chemistry01 natural sciencesInorganic ChemistryStructure-Activity Relationshipchemistry.chemical_compoundCoordination ComplexesCell Line Tumororganometallic compoundsPyridineHumansCytotoxic T cellsytotoksisuusPhysical and Theoretical ChemistryHomolepticCytotoxicityta116Cell ProliferationDose-Response Relationship DrugMolecular Structure010405 organic chemistryNitrosylationCombinatorial chemistry0104 chemical sciencesHEK293 Cellssyöpäsolutchemistrycancer cellsOvarian cancer cellscytotoxicityDrug Screening Assays AntitumorAzo CompoundsPalladiumPalladiumInorganic Chemistry
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Copper Uptake Induces Self-Assembly of 18.5 kDa Myelin Basic Protein (MBP)

2010

Myelin basic protein (MBP) is predominantly found in the membranes of the myelin sheath of the central nervous system and is involved in important protein-protein and protein-lipid interactions in vivo and in vitro. Furthermore, divalent transition metal ions, especially Zn(2+) and Cu(2+), seem to directly affect the MBP-mediated formation and stabilization of the myelin sheath of the central nervous system. MBP belongs to the realm of intrinsically disordered proteins, and only fragmentary information is available regarding its partial structure(s) or supramolecular arrangements. Here, using standard continuous wave and modern pulse electron paramagnetic resonance methods, as well as dynam…

Models Molecularinorganic chemicalsLightBiophysicsSupramolecular chemistryIn Vitro TechniquesIntrinsically disordered proteinsBiophysical PhenomenaDivalentlaw.inventionlawAnimalsScattering RadiationMoleculeParticle SizeElectron paramagnetic resonanceIon transporterchemistry.chemical_classificationIon TransportbiologyProteinElectron Spin Resonance SpectroscopyMyelin Basic ProteinMyelin basic proteinSolutionsZincMembranechemistryBiochemistrybiology.proteinBiophysicsCattleProtein MultimerizationCopperBiophysical Journal
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Structural and functional consequences of the replacement of proximal residues Cys172 and Cys192 in the large subunit of ribulose-1,5-bisphosphate ca…

2008

Proximal Cys(172) and Cys(192) in the large subunit of the photosynthetic enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) are evolutionarily conserved among cyanobacteria, algae and higher plants. Mutation of Cys(172) has been shown to affect the redox properties of Rubisco in vitro and to delay the degradation of the enzyme in vivo under stress conditions. Here, we report the effect of the replacement of Cys(172) and Cys(192) by serine on the catalytic properties, thermostability and three-dimensional structure of Chlamydomonas reinhardtii Rubisco. The most striking effect of the C172S substitution was an 11% increase in the specificity factor when compared wi…

Models Molecularinorganic chemicalsOxygenaseRibulose-Bisphosphate CarboxylaseProtein subunitSpecificity factorChlamydomonas reinhardtiiCrystallography X-RayBiochemistryCatalysischemistry.chemical_compoundEnzyme StabilityAnimalsCysteineMolecular BiologyBinding SitesRibulose 15-bisphosphatebiologyfungiRuBisCOTemperaturefood and beveragesCell Biologybiology.organism_classificationLyaseMolecular biologyProtein Structure TertiaryPyruvate carboxylaseKineticsProtein SubunitsBiochemistrychemistryMutationbiology.proteinChlamydomonas reinhardtiiBiochemical Journal
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Structural mechanism of signal transduction in a phytochrome histidine kinase

2022

AbstractPhytochrome proteins detect red/far-red light to guide the growth, motion, development and reproduction in plants, fungi, and bacteria. Bacterial phytochromes commonly function as an entrance signal in two-component sensory systems. Despite the availability of three-dimensional structures of phytochromes and other two-component proteins, the conformational changes, which lead to activation of the protein, are not understood. We reveal cryo electron microscopy structures of the complete phytochrome from Deinoccocus radiodurans in its resting and photoactivated states at 3.6 Å and 3.5 Å resolution, respectively. Upon photoactivation, the photosensory core module hardly changes its ter…

Models MolecularkinaasitMultidisciplinaryphotochemistryHistidine KinaseLightBacteriaelectron microscopyBiochemistry and Molecular BiologyGeneral Physics and AstronomyelektronimikroskopiaGeneral ChemistryGeneral Biochemistry Genetics and Molecular BiologykinasesBacterial Proteinsplant signalling3111 BiomedicinePhytochromevalokemiaBiokemi och molekylärbiologiSignal Transduction
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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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