Search results for " binding"

showing 10 items of 1758 documents

The Greenland shark Somniosus microcephalus—Hemoglobins and ligand-binding properties

2017

A large amount of data is currently available on the adaptive mechanisms of polar bony fish hemoglobins, but structural information on those of cartilaginous species is scarce. This study presents the first characterisation of the hemoglobin system of one of the longest-living vertebrate species (392 +/- 120 years), the Arctic shark Somniosus microcephalus. Three major hemoglobins are found in its red blood cells and are made of two copies of the same a globin combined with two copies of three very similar beta subunits. The three hemoglobins show very similar oxygenation and carbonylation properties, which are unaffected by urea, a very important compound in marine elasmobranch physiology.…

---0301 basic medicinegenetic structuresProtein ConformationGreenlandlcsh:MedicineRESONANCE RAMAN-SPECTRAHETERODONTUS-PORTUSJACKSONISpectrum Analysis RamanBiochemistrychemistry.chemical_compoundHemoglobinsProtein structureAMINO-ACID SEQUENCEAnimal CellsSequence Analysis ProteinRed Blood CellsUreaNOTOTHENIOID FISHESPost-Translational Modificationlcsh:ScienceHemeChondrichthyesMultidisciplinarybiologyChemistryOrganic CompoundsChemical ReactionsVertebrateEukaryotaMOLECULAR ADAPTATIONSMicrocephalusGlobinsChemistryBiochemistryOptical EquipmentVertebratesPhysical SciencesEngineering and TechnologyCellular TypesResearch ArticleEnvironmental MonitoringProtein BindingQUATERNARY STRUCTURESAllosteric regulationEquipmentSTRETCHING FREQUENCIESHeme03 medical and health sciencesOXYGEN-BINDINGbiology.animalAnimals14. Life underwaterGlobinHemoglobinPhotolysisBlood Cells030102 biochemistry & molecular biologyLaserslcsh:ROrganic ChemistryOrganismsChemical CompoundsBiology and Life SciencesProteinsxxxCell Biologybiology.organism_classificationCARTILAGINOUS FISHOxygen030104 developmental biologySomniosusFishSharkslcsh:QHemoglobinProtein MultimerizationELASMOBRANCH HEMOGLOBINElasmobranchiiPLoS ONE
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Use of Density Functional Based Tight Binding Methods in Vibrational Circular Dichroism.

2018

Vibrational circular dichroism (VCD) is a spectroscopic technique used to resolve the absolute configuration of chiral systems. Obtaining a theoretical VCD spectrum requires computing atomic polar and axial tensors on top of the computationally demanding construction of the force constant matrix. In this study we evaluated a VCD model in which all necessary quantities are obtained with density functional based tight binding (DFTB) theory. The analyzed DFTB parametrizations fail at providing accurate vibrational frequencies and electric dipole gradients but yield reasonable normal modes at a fraction of the computational cost of density functional theory (DFT). Thus, by applying DFTB in comp…

/dk/atira/pure/sustainabledevelopmentgoals/affordable_and_clean_energyChemistryQUÍMICA QUÂNTICA02 engineering and technology010402 general chemistry021001 nanoscience & nanotechnology01 natural sciencesMolecular physicsSpectral line0104 chemical sciencesDipoleTight bindingNormal modeYield (chemistry)Vibrational circular dichroismPolarDensity functional theorySDG 7 - Affordable and Clean EnergyPhysical and Theoretical Chemistry0210 nano-technologyThe journal of physical chemistry. A
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MD Simulation Investigation on the Binding Process of Smoke-Derived Germination Stimulants to Its Receptor

2019

Karrikins (KARs) are a class of smoke-derived seed germination stimulants with great significance in both agriculture and plant biology. By means of direct binding to the receptor protein KAI2, the compounds can initiate the KAR signal transduction pathway, hence triggering germination of the dormant seeds in the soil. In the research, several molecular dynamics (MD) simulation techniques were properly integrated to investigate the binding process of KAR1 to KAI2 and reveal the details of the whole binding event. The calculated binding free energy, -7.00 kcal/mol, is in good agreement with the experimental measurement, -6.83 kcal/mol. The obtained PMF profile indicates the existence of thre…

010304 chemical physicsProtein ConformationChemistryGeneral Chemical EngineeringGerminationGeneral ChemistryPlasma protein bindingMolecular Dynamics SimulationLibrary and Information SciencesLigand (biochemistry)01 natural sciences0104 chemical sciencesComputer Science Applications010404 medicinal & biomolecular chemistryMolecular dynamicsProtein structure0103 physical sciencesMoleBiophysicsThermodynamicsMoleculeSignal transductionReceptorPlant ProteinsProtein BindingJournal of Chemical Information and Modeling
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Oxoanion binding to a cyclic pseudopeptide containing 1,4-disubstituted 1,2,3-triazole moieties

2016

A macrocyclic pseudopeptide 3 is described featuring three amide groups and three 1,4-disubstituted 1,2,3-triazole units along the ring. This pseudopeptide was designed such that the amide NH groups and the triazole CH groups converge toward the cavity, thus creating an environment well suited for anion recognition. Conformational studies in solution combined with X-ray crystallography confirmed this preorganisation. Solubility of 3 restricted binding studies to organic media such as 5 vol% DMSO/acetone or DMSO/water mixtures with a water content up to 5 vol%. These binding studies demonstrated that 3 binds to a variety of inorganic anions in DMSO/acetone including chloride, nitrate, sulfat…

010405 organic chemistryChemistryStereochemistryDimerOrganic ChemistryTriazoleoxoanion bindings010402 general chemistry01 natural sciencesBiochemistryChlorideMedicinal chemistry0104 chemical scienceschemistry.chemical_compoundpseudopeptidesStability constants of complexesAmidemedicineMoleculePhysical and Theoretical ChemistrySulfateSolubilityta116medicine.drugOrganic & Biomolecular Chemistry
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Solution Conformation and Self‐Assembly of Ferrocenyl(thio)ureas

2016

Conformations and (dis)assembly processes of ureas and thioureas are of fundamental importance in supramolecular chemistry, anion binding, or crystal engineering, both in solution and in the solid state. For sensing and switching processes a redox-active unit, such as the ferrocene/ferrocenium couple, is especially suitable. Here, self-assembly processes of redox-active ferrocenyl(thio)ureas FcNHC(X)NHR [X = O, R = Fc (1), Ph (2), 1-naphthyl (3), Me (4), Et (5); X = S, R = Fc (6), 1-anthracenyl (7)] through hydrogen bonds – both in the solid state and in THF and CH2Cl2 solution – are reported. Special emphasis is placed on the impact of nonclassical intramolecular NH···Fe hydrogen bonds in …

010405 organic chemistryHydrogen bondStereochemistrySupramolecular chemistryThio-010402 general chemistryCrystal engineering01 natural sciencesRedox0104 chemical sciencesInorganic Chemistrychemistry.chemical_compoundCrystallographyFerrocenechemistryIntramolecular forceAnion bindingEuropean Journal of Inorganic Chemistry
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Macrocyclic complexes based on [N⋯I⋯N]+ halogen bonds

2021

New 1–2 nm macrocyclic iodine(I) complexes prepared VIA a simple ligand exchange reaction manifest rigid 0.5–1 nm cavities that bind the hexafluorophosphate anion in the gas phase. The size of the cavities and the electrostatic interactions with the iodine(I) cations influence the anion binding properties of these macrocyclic complexes.

010405 organic chemistryLigandMetals and Alloyschemistry.chemical_elementGeneral Chemistry010402 general chemistryElectrostaticsIodine01 natural sciencesCatalysis0104 chemical sciences3. Good healthSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsIonGas phasechemistry.chemical_compoundchemistryHexafluorophosphatePolymer chemistryHalogenMaterials ChemistryCeramics and CompositesAnion bindingChemical Communications
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Metal Complexes of Two Specific Regions of ZnuA, a Periplasmic Zinc(II) Transporter from Escherichia coli

2020

The crystal structure of ZnZnuA from Escherichia coli reveals two metal binding sites. (i) The primary binding site, His143, is located close the His-rich loop (residues 116-138) and plays a significant role in Zn(II) acquisition. (ii) The secondary binding site involves His224. In this work, we focus on understanding the interactions of two metal ions, Zn(II) and Cu(II), with two regions of ZnuA, which are possible anchoring sites for Zn(II): Ac-115MKSIHGDDDDHDHAEKSDEDHHHGDFNMHLW145-NH2 (primary metal binding site) and Ac-223GHFTVNPEIQPGAQRLHE240-NH2 (secondary metal binding site). The histidine-rich loop (residues 116-138) has a role in the capture of zinc(II), which is then further deliv…

010405 organic chemistryStereochemistryChemistrychemistry.chemical_elementMetal Binding SitePeriplasmic spaceZinc010402 general chemistryLigand (biochemistry)01 natural sciences0104 chemical sciencesInorganic ChemistryMetalchemistry.chemical_compoundvisual_artvisual_art.visual_art_mediumImidazolePhysical and Theoretical ChemistryBinding siteHistidine
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Role of Bacillus thuringiensis Cry1A toxins domains in the binding to the ABCC2 receptor from Spodoptera exigua

2018

Abstract Cry proteins from Bacillus thuringiensis (Bt) have been used to control insect pests either as formulated sprays or as in Bt-crops. However, field-evolved resistance to Bt proteins is threatening the long-term use of Bt products. The SeABCC2 locus has been genetically linked to resistance to a Bt bioinsecticide (Xentari™) in Spodoptera exigua (a mutation producing a truncated form of the transporter lacking an ATP binding domain was found in the resistant insects). Here, we investigated the role of SeABCC2 in the mode of action of Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ca, and two Cry1A-1Ca hybrids by expressing the receptor in Sf21 and HEK293T cell lines. Cell toxicity assays showed that Sf2…

0106 biological sciences0301 basic medicineCell SurvivalBacillus thuringiensisGene ExpressionSpodopteraSpodopteraTransfection01 natural sciencesBiochemistryHemolysin ProteinsStructure-Activity Relationship03 medical and health sciencesBacterial ProteinsProtein DomainsBacillus thuringiensisExiguaSf9 CellsAnimalsHumansProtein IsoformsBinding siteReceptorMolecular BiologySf21Binding SitesBacillus thuringiensis Toxinsbiologyfungibiology.organism_classificationMultidrug Resistance-Associated Protein 2Recombinant ProteinsClone CellsEndotoxins010602 entomologyHEK293 Cells030104 developmental biologyBiochemistryCry1AcLarvaInsect ScienceMutationInsect ProteinsMultidrug Resistance-Associated ProteinsPlasmidsProtein BindingBinding domainInsect Biochemistry and Molecular Biology
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The Odorant-Binding Proteins of the Spider Mite Tetranychus urticae

2021

Spider mites are one of the major agricultural pests, feeding on a large variety of plants. As a contribution to understanding chemical communication in these arthropods, we have characterized a recently discovered class of odorant-binding proteins (OBPs) in Tetranychus urticae. As in other species of Chelicerata, the four OBPs of T. urticae contain six conserved cysteines paired in a pattern (C1–C6, C2–C3, C4–C5) differing from that of insect counterparts (C1–C3, C2–C5, C4–C6). Proteomic analysis uncovered a second family of OBPs, including twelve members that are likely to be unique to T. urticae. A three-dimensional model of TurtOBP1, built on the recent X-ray structure of Varroa destruc…

0106 biological sciences0301 basic medicineModels MolecularProteomicsProteomeOdorant bindingProtein ConformationInsectLigandsReceptors Odorant01 natural scienceschemistry.chemical_compoundTetranychus urticaeBiology (General)SpectroscopyPhylogenymedia_commonmass spectrometryGeneticsbiologyligand-bindingMolecular Structurespider mitesGeneral MedicineTetranychus urticaeComputer Science ApplicationsChemistryConiferyl aldehydedisulfide bridgesTetranychidaeProtein Bindingspider mites.QH301-705.5media_common.quotation_subjectodorant-binding proteinsCatalysisArticleInorganic Chemistry03 medical and health sciencesSpider mite<i>Tetranychus urticae</i>AnimalsAmino Acid SequencePhysical and Theoretical ChemistryQD1-999Molecular BiologySpiderOrganic Chemistrybiology.organism_classification010602 entomology030104 developmental biologychemistryVarroa destructorOdorantsChelicerataInternational Journal of Molecular Sciences
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Functional characterization of the chaperon-like protein Cdc48 in cryptogein-induced immune response in tobacco

2017

SPEIPMUBINRASUPDATDOCT; Cdc48, a molecular chaperone conserved in different kingdoms, is a member of the AAA+ family contributing to numerous processes in mammals including proteins quality control and degradation, vesicular trafficking, autophagy and immunity. The functions of Cdc48 plant orthologues are less understood. We previously reported that Cdc48 is regulated by S-nitrosylation in tobacco cells undergoing an immune response triggered by cryptogein, an elicitin produced by the oomycete Phytophthora cryptogea. Here, we inv estigated the function of NtCdc48 in cryptogein signalling and induced hypersensitive-like cell death. NtCdc48 was found to accumulate in elicited cells at both th…

0106 biological sciences0301 basic medicineProgrammed cell deathPhysiologyImmunoprecipitationNitrosation[SDV]Life Sciences [q-bio]PopulationPlant ScienceBiologyBioinformatics01 natural sciencesdefence responsescryptogeinFungal Proteins03 medical and health sciencesImmune systemGene Expression Regulation PlantValosin Containing ProteinPlant CellsTobaccoRNA MessengereducationPlant ProteinsRegulation of gene expressioneducation.field_of_studyFungal protein[ SDV ] Life Sciences [q-bio]AutophagyElicitinCell biology030104 developmental biologycell deathChromatography GelCdc48 partnersNtCdc48Protein Binding010606 plant biology & botany
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