Search results for "Models"

showing 10 items of 8211 documents

A Janus-Faced IM30 Ring Involved in Thylakoid Membrane Fusion Is Assembled from IM30 Tetramers.

2017

Summary Biogenesis and dynamics of thylakoid membranes likely involves membrane fusion events. Membrane attachment of the inner membrane-associated protein of 30 kDa (IM30) affects the structure of the lipid bilayer, finally resulting in membrane fusion. Yet, how IM30 triggers membrane fusion is largely unclear. IM30 monomers pre-assemble into stable tetrameric building blocks, which further align to form oligomeric ring structures, and differently sized IM30 rings bind to membranes. Based on a 3D reconstruction of IM30 rings, we locate the IM30 loop 2 region at the bottom of the ring and show intact membrane binding but missing fusogenic activity of loop 2 mutants. However, helix 7, which …

0301 basic medicineModels MolecularChemistryPeripheral membrane proteinLipid bilayer fusionBiological membraneMembrane FusionThylakoidsTransmembrane protein03 medical and health sciencesCrystallographyChloroplast Proteins030104 developmental biologyMembraneStructural BiologyMembrane biogenesisLiposomesBiophysicsProtein MultimerizationLipid bilayerMolecular BiologyIntegral membrane proteinProtein BindingStructure (London, England : 1993)
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High-Pressure-Driven Reversible Dissociation of α-Synuclein Fibrils Reveals Structural Hierarchy

2017

The analysis of the α-synuclein (aS) aggregation process, which is involved in Parkinson's disease etiopathogenesis, and of the structural feature of the resulting amyloid fibrils may shed light on the relationship between the structure of aS aggregates and their toxicity. This may be considered a paradigm of the ground work needed to tackle the molecular basis of all the protein-aggregation-related diseases. With this aim, we used chemical and physical dissociation methods to explore the structural organization of wild-type aS fibrils. High pressure (in the kbar range) and alkaline pH were used to disassemble fibrils to collect information on the hierarchic pathway by which distinct β-sh…

0301 basic medicineModels MolecularCircular dichroismAmyloidProtein FoldingProtein domainBeta sheetBiophysicsFibrilMicroscopy Atomic ForceSpectrum Analysis RamanDissociation (chemistry)03 medical and health sciences0302 clinical medicineProtein structureMicroscopy Electron TransmissionProtein DomainsSpectroscopy Fourier Transform InfraredEscherichia coliPressureChemistryCircular DichroismEnergy landscapeProteinsalpha synuclein amyloid recombinant proteinHydrogen-Ion ConcentrationRecombinant ProteinsCrystallography030104 developmental biologyMutationalpha-SynucleinProtein foldingProtein Conformation beta-StrandProtein Multimerization030217 neurology & neurosurgery
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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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pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin

2017

Infrared spectroscopy has been used in the past to probe the dynamics of internal proton transfer reactions taking place during the functional mechanism of proteins but has remained mostly silent to protonation changes in the aqueous medium. Here, by selectively monitoring vibrational changes of buffer molecules with a temporal resolution of 6 µs, we have traced proton release and uptake events in the light-driven proton-pump bacteriorhodopsin and correlate these to other molecular processes within the protein. We demonstrate that two distinct chemical entities contribute to the temporal evolution and spectral shape of the continuum band, an unusually broad band extending from 2,300 to well…

0301 basic medicineModels MolecularCytoplasmNuclear TheoryMolecular ConformationInfrared spectroscopyIonic bondingProtonationBuffers010402 general chemistry53001 natural sciences03 medical and health sciencesDeprotonationSpectroscopy Fourier Transform InfraredMoleculeNuclear ExperimentMultidisciplinarybiologyChemistryWaterBacteriorhodopsinHydrogen-Ion Concentration0104 chemical sciencesKinetics030104 developmental biologyPNAS PlusChemical physicsCytoplasmTemporal resolutionBacteriorhodopsinsbiology.proteinPhysics::Accelerator PhysicsProtonsMetabolic Networks and PathwaysProtein Binding
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Addition of thiols to the double bond of dipeptide C-terminal dehydroalanine as a source of new inhibitors of cathepsin C.

2017

Addition of thiols to double bond of glycyl-dehydroalanine and phenyl-dehydroalanine esters provided micromolar inhibitors of cathepsin C. The structure-activity studies indicated that dipeptides containing N-terminal phenylalanine exhibit higher affinity towards the enzyme. A series of C-terminal S-substituted cysteines are responsible for varying interaction with S1 binding pocket of cathepsin C. Depending on diastereomer these compounds most likely act as slowly reacting substrates or competitive inhibitors. This was proved by TLC analysis of the medium in which interaction of methyl (S)-phenylalanyl-(R,S)-(S-adamantyl)cysteinate (7i) with the enzyme was studied. Molecular modeling enabl…

0301 basic medicineModels MolecularDouble bondStereochemistryPhenylalanineCysteine Proteinase InhibitorsBiochemistryCathepsin CCathepsin CSubstrate Specificity03 medical and health scienceschemistry.chemical_compoundStructure-Activity Relationship0302 clinical medicineDehydroalanineMoietyAnimalsSulfhydryl CompoundsBinding sitechemistry.chemical_classificationDipeptideAlanineBinding SitesDehydropeptidesDiastereomerEnzyme inhibitorsGeneral MedicineDipeptidesKinetics030104 developmental biologychemistryThiol addition030220 oncology & carcinogenesisCattleBiochimie
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Incorporation of mRNA in Lamellar Lipid Matrices for Parenteral Administration

2018

Molecular pharmaceutics 15(2), 642 - 651 (2018). doi:10.1021/acs.molpharmaceut.7b01022

0301 basic medicineModels MolecularDrug CompoundingKineticsLipid BilayersPharmaceutical Science610TransfectionCell LineMyoblasts03 medical and health sciencesMiceX-Ray DiffractionCationsDrug DiscoveryScattering Small AngleAnimalsRNA Messengerddc:610Lipid bilayerLuciferasesMessenger RNALiposomeDrug CarriersChemistryAqueous two-phase systemRNATransfection030104 developmental biologyDelayed-Action PreparationsLiposomesBiophysicsMolecular Medicinelipids (amino acids peptides and proteins)Drug carrier
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Probing Differential Binding Mechanisms of Phenylalanine-Glycine-Rich Nucleoporins by Single-Molecule FRET

2018

Abstract Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex. They are highly dynamic under physiological conditions and studying their interaction with nuclear transport receptors (NTRs) is key to understanding the molecular mechanism of nucleocytoplasmic transport. Distinct conformational features of FG-Nups interacting with diverse NTRs can be detected by multiparameter single-molecule fluorescence energy transfer (smFRET), which is a powerful technique for studying the dynamics and interactions of biomolecules in solution. Here we provide a detailed protocol utilizing smFRET to reveal dif…

0301 basic medicineModels MolecularGlycosylationProtein ConformationPhenylalanineGlycineIntrinsically disordered proteinsArticle03 medical and health scienceschemistry.chemical_compoundFluorescence Resonance Energy TransferAnimalsHumansNuclear porechemistry.chemical_classificationBiomoleculeSingle-molecule FRETEquipment DesignIntrinsically Disordered ProteinsNuclear Pore Complex Proteins030104 developmental biologychemistryNucleocytoplasmic TransportBiophysicsNucleoporinNuclear transportProtein BindingIntrinsically Disordered Proteins
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Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors

2018

Summary Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an “archetypal-fuzzy” complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lowe…

0301 basic medicineModels MolecularGlycosylationglycosylationProtein ConformationPhenylalanineGlycineSequence (biology)Intrinsically disordered proteinsnuclear transport receptorssingle-molecule FRETGeneral Biochemistry Genetics and Molecular BiologyArticle03 medical and health scienceschemistry.chemical_compound0302 clinical medicineEscherichia coliFluorescence Resonance Energy TransferHumansNuclear poreReceptorlcsh:QH301-705.5Single-molecule FRETmolecular dynamics simulationsbinding mechanismintrinsically disordered proteinFG-Nup3. Good healthNuclear Pore Complex Proteins030104 developmental biologychemistrylcsh:Biology (General)BiophysicsNuclear PoreNucleoporinNuclear transport030217 neurology & neurosurgeryProtein BindingCell Reports
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Prefolded Synthetic G-Quartets Display Enhanced Bioinspired Properties

2016

International audience; A water-soluble template-assembled synthetic G-quartet (TASQ) based on the use of a macrocyclodecapeptide scaffold was designed to display stable intramolecular folds alone in solution. The preformation of the guanine quartet, demonstrated by NMR and CD investigations, results in enhanced peroxidase-type biocatalytic activities and improved quadruplex-interacting properties. Comparison of its DNAzyme-boosting properties with the ones of previously published TASQ revealed that, nowadays, it is the best DNAzyme-boosting agent.

0301 basic medicineModels MolecularGuanineStereochemistryDNAzymewaterSupramolecular chemistryDeoxyribozymednainsights010402 general chemistryG-QuartetsG-quadruplexchemistry[ CHIM ] Chemical Sciences01 natural sciencesCatalysissupramolecular chemistryg-quadruplex structures03 medical and health scienceschemistry.chemical_compoundG-quartets[CHIM]Chemical SciencesrnaComputingMilieux_MISCELLANEOUSligandsbiologyOrganic Chemistry[CHIM.CATA]Chemical Sciences/CatalysisGeneral ChemistryDNA CatalyticSmall moleculeG-quadruplexes0104 chemical sciencesSolutionssmall molecules030104 developmental biologychemistryBiocatalysisIntramolecular forceBiocatalysisNucleic Acid Conformationcyclodecapeptideacid
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Sensory domain contraction in histidine kinase CitA triggers transmembrane signaling in the membrane-bound sensor

2017

Bacteria use membrane-integral sensor histidine kinases (HK) to perceive stimuli and transduce signals from the environment to the cytosol. Information on how the signal is transmitted across the membrane by HKs is still scarce. Combining both liquid- and solid-state NMR, we demonstrate that structural rearrangements in the extracytoplasmic, citrate-sensing Per-Arnt-Sim (PAS) domain of HK CitA are identical for the isolated domain in solution and in a longer construct containing the membrane-embedded HK and lacking only the kinase core. We show that upon citrate binding, the PAS domain contracts, resulting in a shortening of the C-terminal β-strand. We demonstrate that this contraction of t…

0301 basic medicineModels MolecularHistidine Kinase030106 microbiologyMolecular ConformationCitric Acid03 medical and health sciencesStructure-Activity RelationshipBacterial ProteinsPAS domainProtein Interaction Domains and MotifsAmino Acid SequenceHistidineMultidisciplinaryChemistryKinaseHistidine kinaseGeobacillusMembrane ProteinsBiological SciencesTransmembrane proteinCell biologyCytosolHelixSignal transductionProtein BindingSignal Transduction
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