Search results for "kristallografia"

showing 10 items of 64 documents

Skeletal Dysplasia Mutations Effect on Human Filamins’ Structure and Mechanosensing

2016

AbstractCells’ ability to sense mechanical cues in their environment is crucial for fundamental cellular processes, leading defects in mechanosensing to be linked to many diseases. The actin cross-linking protein Filamin has an important role in the conversion of mechanical forces into biochemical signals. Here, we reveal how mutations in Filamin genes known to cause Larsen syndrome and Frontometaphyseal dysplasia can affect the structure and therefore function of Filamin domains 16 and 17. Employing X-ray crystallography, the structure of these domains was first solved for the human Filamin B. The interaction seen between domains 16 and 17 is broken by shear force as revealed by steered mo…

0301 basic medicineFilaminsScienceProtein domainPeptide bindingPlasma protein bindingmacromolecular substancesBiologyMolecular Dynamics SimulationFilaminmedicine.disease_causeBioinformaticsCrystallography X-RayOsteochondrodysplasiasMechanotransduction CellularArticlecomputational biophysics03 medical and health sciences0302 clinical medicineProtein DomainsmedicineHumansLarsen syndromeForeheadMechanotransductionNMR-spektroskopiaActinMutationMultidisciplinaryBinding SitesQRSAXSmedicine.diseasecytoskeletal proteinsActinsCell biologybody regions030104 developmental biologyMutationMedicine030217 neurology & neurosurgeryröntgenkristallografiaProtein Binding
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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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Ultrafast structural changes within a photosynthetic reaction centre

2021

Nature <London> / Physical science 589, 310 - 314 (2021). doi:10.1038/s41586-020-3000-7

0301 basic medicinePhotosynthetic reaction centreChlorophyllModels MolecularklorofylliCytoplasmUbiquinonePhotosynthetic Reaction Center Complex ProteinsElectrons02 engineering and technologyPhotochemistrymedicine.disease_cause530yhteyttäminenbakteeritElectron Transport03 medical and health sciencesElectron transfermedicineMoleculeddc:530BacteriochlorophyllsbioenergetiikkaComputingMilieux_MISCELLANEOUSHyphomicrobiaceaeMultidisciplinaryBinding SitesCrystallography[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry Molecular Biology/Structural Biology [q-bio.BM]ChemistryBlastochloris viridisLaserskalvot (biologia)PheophytinsBiological membraneVitamin K 2021001 nanoscience & nanotechnologyAcceptor030104 developmental biologyPicosecondFemtosecondsense organsProtons0210 nano-technologyOxidation-Reductionröntgenkristallografia
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Base-Controlled Regiospecific Mono-Benzylation/Allylation and Diallylation of 4-Aryl-5-indolyl-1,2,4-triazole-3-thione : Thio-Aza Allyl Rearrangement

2023

The regiospecific S-benzylation/allylation of two 4-aryl-5-indolyl-1,2,4-triazole-3-thione precursors was carried out using Et3N as a base. Allyl group migration from exocyclic sulfur to the triazole nitrogen (N3) was successfully achieved in a short time via thermal fusion without the need for any catalyst. The allylation of indole nitrogen, along with exocyclic sulfur or triazole nitrogen (N3), was carried out using K2CO3 as stronger base. S,N-Diallylated products were converted to N,N-diallylated analogues using a simple fusion approach. Structural analyses of the two newly synthesized hybrids 2b and 5b investigated via the X-ray diffraction of a single crystal combined with Hirshfeld ca…

124-triazole-3-thioneX-ray single-crystal analysisthio-aza allyl rearrangementheterosykliset yhdisteetallylationorgaaniset yhdisteetröntgenkristallografia
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Spectroscopic, crystal structural, theoretical and biological studies of phenylacetohydrazide Schiff base derivatives and their copper complexes

2020

Two phenylacetohydrazide Schiff base derivatives: N’-(1-(2-hydroxyphenyl)ethylidene)-2-phenylacetohydrazide, HL1, and N’-((1-hydroxynaphthalen-2-yl)methylene)-2-phenylacetohydrazide, HL2, were synthesized. HL1 dimerizes in presence of HCl, probably via radical mechanism to give (2,2’-((1E)-hydrazine-1,2-diylidenebis(ethan-1-yl-1-ylidene))diphenol (DIM). Thermal reactions of Cu(II) ions with the two Schiff base ligands resulted in formation of the binuclear complexes [(CuL1)2] and [(CuL2)2]. The stoichiometry and structures of the reported compounds were investigated by several spectroscopic and analytical techniques. The structure of the HL1 ligand and its complex [(CuL1)2] as well as the D…

CT-DNA bindingantioxidant activitychemistry.chemical_elementkupari010402 general chemistry01 natural sciencesAnalytical ChemistryInorganic Chemistrykemialliset sidoksetchemistry.chemical_compoundDFT studiesReactivity (chemistry)copper complexesMethyleneSpectroscopyantioksidantitSchiff base010405 organic chemistryLigandtiheysfunktionaaliteoriaOrganic Chemistrymolecular dockingkompleksiyhdisteetCopper0104 chemical sciencesCrystallographyMolecular geometrychemistrySingle crystalröntgenkristallografiaStoichiometryX-ray analysisJournal of Molecular Structure
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Cation binding resorcinarene bis-crowns: the effect of lower rim alkyl chain length on crystal packing and solid lipid nanoparticles

2012

A group of seven resorcinarene bis-crown ethers (CNBC5) with two polyether bridges at the upper rim and either propyl, butyl, pentyl, heptyl, nonyl, decyl or undecyl groups at the lower rim were synthesized and their binding properties with Cs+ were investigated by NMR titration. The bis-crowns form 1:2 complexes with Cs+ with binding constants of logK 4–5. Crystal structures of bis-crowns and their Cs+ and K+ complexes were studied and different packing motifs were found depending on the alkyl chain length. Short ethyl, propyl and butyl alkyl chains gave a layer or pillar packing where the polar and non-polar regions cannot be distinguished, whereas longer pentyl and decyl chains formed bi…

Cation bindingkaliumStereochemistryydinmagneettinen resonanssiCyclohexane conformationsolid lipid nanoparticleamphiphileCrystal structureCatalysisCrystalcesiumAmphiphilesupramolekyylikemiaMaterials Chemistrykiinteä lipidipartikkelisupramolekulaarinen kemiaMoleculemacrocyclic compoundta116Alkylkaliksareeniitsejärjestäytyminenchemistry.chemical_classificationresorcinareneChemistryGeneral Chemistrycaesiumself-assemblyResorcinarenekompleksiCrystallographynuclear magnetic resonanceamfifiilimakrosyklinen yhdistecalixarenecomplexröntgenkristallografiaresorsinareeni
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The primary structural photoresponse of phytochrome proteins captured by a femtosecond X-ray laser

2019

Phytochrome proteins control the growth, reproduction, and photosynthesis of plants, fungi, and bacteria. Light is detected by a bilin cofactor, but it remains elusive how this leads to activation of the protein through structural changes. We present serial femtosecond X-ray crystallographic data of the chromophore-binding domains of a bacterial phytochrome at delay times of 1 ps and 10 ps after photoexcitation. The data reveal a twist of the D-ring, which leads to partial detachment of the chromophore from the protein. Unexpectedly, the conserved so-called pyrrole water is photodissociated from the chromophore, concomitant with movement of the A-ring and a key signaling aspartate. The chan…

DYNAMICSQH301-705.5ScienceEXCITED-STATEDIFFRACTION010402 general chemistryPhotosynthesisphytochromes01 natural sciencesCofactor03 medical and health scienceschemistry.chemical_compoundDeinococcus radioduransPROTON-TRANSFERREVEALSSFXCRYSTAL-STRUCTUREBiology (General)Bilin030304 developmental biologyISOMERIZATION0303 health sciencesbiologyPhytochromeD-RINGChemistryCRYSTALLOGRAPHYinitial photoresponsQRChromophore0104 chemical sciencesPhotoexcitationFemtosecondbiology.proteinBiophysics1182 Biochemistry cell and molecular biologyMedicine3111 BiomedicinevalokemiaproteiinitSignal transductionröntgenkristallografia
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Thermal, spectroscopic and crystallographic analysis of mannose-derived linear polyols

2018

The major diastereomer formed in the Barbier-type metal-mediated allylation of D-mannose has previously been shown to adopt a perfectly linear conformation, both in solid state and in solution, resulting in the formation of hydrogen-bonded networks and subsequent aggregation from aqueous solution upon stirring. Here, a comprehensive study of the solid state structure of both the allylated D-mannose and its racemic form has been conducted. The binary melting point diagram of the system was determined by differential scanning calorimetry analysis, and the obtained results, along with structure determination by single crystal X-ray diffraction, confirmed that allylated mannose forms a true rac…

DiffractionMaterials science010402 general chemistry01 natural sciencesDifferential scanning calorimetryNMR spectroscopycrystalsGeneral Materials SciencekalorimetriaNMR-spektroskopiata116x-ray crystallographyAqueous solution010405 organic chemistryDiastereomerGeneral ChemistryCondensed Matter Physicskiteet0104 chemical sciencessokerialkoholitCrystallographysugar alcoholsPolymorphism (materials science)Melting pointEnantiomerSingle crystalcalorimetryröntgenkristallografia
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Non-syndromic Mitral Valve Dysplasia Mutation Changes the Force Resilience and Interaction of Human Filamin A

2018

International audience; Filamin A (FLNa), expressed in endocardial endothelia during fetal valve morphogenesis, is key in cardiac development. Missense mutations in FLNa cause non-syndromic mitral valve dysplasia (FLNA-MVD). Here, we aimed to reveal the currently unknown underlying molecular mechanism behind FLNA-MVD caused by the FLNa P637Q mutation. The solved crystal structure of the FLNa3-5 P637Q revealed that this mutation causes only minor structural changes close to mutation site. These changes were observed to significantly affect FLNa's ability to transmit cellular force and to interact with its binding partner. The performed steered molecular dynamics simulations showed that signi…

Filamins[SDV]Life Sciences [q-bio]Protein Tyrosine Phosphatase Non-Receptor Type 12Heart Valve DiseasesMutation MissenseMorphogenesisProtein tyrosine phosphataseMolecular Dynamics SimulationBiologyFilaminta3111ArticleFLNA-MVD03 medical and health sciencessteered molecular dynamics simulationsStructural Biologymechanical forcesmedicineHumansMitral valve prolapseMissense mutationFLNAmolekyylidynamiikkasydäntauditCell adhesionMolecular Biology030304 developmental biologyX-ray crystallography0303 health sciencesBinding Sites030302 biochemistry & molecular biologyta1182filamiinitprotein tyrosine phosphatase 12medicine.disease3. Good healthCell biologyFilamin AMutation (genetic algorithm)cardiovascular systemMitral Valveproteiinitmitral valve prolapseröntgenkristallografiaProtein Binding
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Synthesis, X-ray Structure, Conformational Analysis, and DFT Studies of a Giant s-Triazine bis-Schiff Base

2021

The current work involves the synthesis of 2,2′-(6-(piperidin-1-yl)-1,3,5-triazine-2,4-diyl)bis(hydrazin-2-yl-1-ylidene))bis(methanylylidene))diphenol 4, characterization, and the DFT studies of the reported compound. The crystal unit cell parameters of 4 are a = 8.1139(2) Å, b = 11.2637(2) Å, c = 45.7836(8) Å. The unit cell volume is 4184.28(15) Å3 and Z = 4. It crystallized in the orthorhombic crystal system and Pbca space group. The O…H, N…H, C…H, H…H and C…C intermolecular contacts which affect the crystal stability were quantitatively analyzed using Hirshfeld calculations. Their percentages were calculated to be 9.8, 15.8, 23.7, 46.4, and 1.6% from the whole contacts occurred in the cr…

General Chemical EngineeringInorganic ChemistryCrystalchemistry.chemical_compounds-triazineNBOGeneral Materials Sciencebis-Schiff basetyppiyhdisteetheterosykliset yhdisteetConformational isomerismkemiallinen synteesiSchiff baseCrystallography<i>s</i>-triazineChemistryHydrogen bondtiheysfunktionaaliteoriaIntermolecular forceconformational analysisHirshfeld analysiskiteetCondensed Matter Physics<i>bis</i>-Schiff baseCrystallographyQD901-999Intramolecular forceOrthorhombic crystal systemröntgenkristallografiaNatural bond orbitalCrystals
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