Search results for "ALANINE"

showing 10 items of 499 documents

Site-by-site tracking of signal transduction in an azidophenylalanine-labeled bacteriophytochrome with step-scan FTIR spectroscopy

2021

Signal propagation in photosensory proteins is a complex and multidimensional event. Unraveling such mechanisms site-specifically in real time is an eligible but a challenging goal. Here, we elucidate the site-specific events in a red-light sensing phytochrome using the unnatural amino acid azidophenylalanine, vibrationally distinguishable from all other protein signals. In canonical phytochromes, signal transduction starts with isomerization of an excited bilin chromophore, initiating a multitude of processes in the photosensory unit of the protein, which eventually control the biochemical activity of the output domain, nanometers away from the chromophore. By implementing the label in pri…

Models MolecularAzidesProtein ConformationPhenylalaninespektroskopiaTongue regionGeneral Physics and Astronomyfotobiologia010402 general chemistryTracking (particle physics)01 natural sciences03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsSpectroscopy Fourier Transform InfraredAmino Acid SequenceAmino AcidsPhysical and Theoretical ChemistryFourier transform infrared spectroscopyBilin030304 developmental biology0303 health sciencesBinding SitesStaining and LabelingbiologyPhytochromeChemistryDeinococcus radioduransChromophorePhotochemical Processesbiology.organism_classification0104 chemical sciencesKineticsBiophysicsPhytochromeproteiinitvalokemiaSignal transductionProtein BindingSignal TransductionPhysical Chemistry Chemical Physics
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Identification of residues in the putative 5th helical region of human interleukin-6, important for activation of the IL-6 signal transducer, gp130

1996

AbstractWe have previously shown that L58 in the putative 5th helical region of human interleukin-6 (IL-6) is important for activation of the IL-6 signal transducer gp130 [de Hon et al. (1995) FEBS Lett. 369, 187–191]. To further explore the importance of individual residues in this region for gp130 activation we have now combined Ala substitutions of residues E52, S53, S54, K55, E56, L58 and E60 with other substitutions in IL-6, known to affect gp130 activation (Q160E and T163P). The combination mutant protein with L58A completely lost the capacity to induce the proliferation of XG-1 myeloma cells, and could effectively antagonize wild type IL-6 activity on these cells. Moreover, the data …

Models MolecularBiophysicsHuman Interleukin-6BiochemistryProtein Structure SecondaryStructure-function analysisgp130Signal Transducer gp130Antigens CDStructural BiologyMutant proteinCytokine Receptor gp130Escherichia coliTumor Cells CulturedGeneticsHumansPoint MutationCloning MolecularInterleukin 6Molecular BiologyAlanineMembrane GlycoproteinsbiologyInterleukin-6Wild typeCell BiologyGlycoprotein 130Recombinant ProteinsProtein Structure TertiaryCell biologyKineticsBiochemistryMutagenesis Site-Directedbiology.proteinLeukemia Erythroblastic AcuteMultiple MyelomaCell DivisionSignal TransductionFEBS Letters
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Density functional study of Cu2+-phenylalanine complex under micro-solvation environment

2013

Abstract We present an atomistic study carried out using density functional calculations including structural relaxations and Car–Parrinello Molecular Dynamics (CPMD) simulations, aiming to investigate the structures of phenylalanine-copper (II) ([Phe-Cu] 2+ ) complexes and their micro-solvation processes. The structures of the [Phe-Cu] 2+ complex with up to four water molecules are optimized using the B3LYP/6-311++G** model in gas phase to identify the lowest energy structures at each degree of solvation ( n  = 0–4). It is found that the phenylalanine appears to be in the neutral form in isolated and mono-hydrated complexes, but in the zwitterionic form in other hydrated complexes (with n …

Models MolecularCar–Parrinello molecular dynamicsPhenylalanineMolecular ConformationDFTMolecular dynamicsMaterials ChemistryMicro-solvationMoleculePhysical and Theoretical ChemistryPhenylalanine-copper (II) complexStructural motifta116Spectroscopyta114LigandHydrogen bondChemistrySolvationHydrogen BondingComputer Graphics and Computer-Aided DesignCrystallographySolvation shellModels ChemicalCPMDCopperJOURNAL OF MOLECULAR GRAPHICS AND MODELLING
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Size- and Structure-Selective Noncovalent Recognition of Saccharides by Tetraethyl and Tetraphenyl Resorcinarenes in the Gas Phase

2008

The noncovalent complexation of tetraethyl and tetraphenyl resorcinarenes with mono-, di-, and oligosaccharides was studied with negative-polarization electrospray ionization quadrupole ion trap and electrospray ionization Fourier-transform ion cyclotron resonance mass-spectrometric analysis. The saccharides formed 1:1 complexes with deprotonated resorcinarenes, which exhibited clear size and structure selectivity in their complexation. In the case of the monosaccharides, hexoses formed much more abundant and kinetically stable complexes than pentoses or deoxyhexoses. A comparison of the mono-, di-, and oligosaccharides revealed that both the relative abundance and stability of the complexe…

Models MolecularCellobiosePhenylalanineElectrospray ionizationCarbohydratesCrystallography X-RayMass spectrometryMass SpectrometryCatalysisSubstrate SpecificityDeprotonationPolymer chemistryCarbohydrate ConformationOrganic chemistryQuadrupole ion trapHost–guest chemistrychemistry.chemical_classificationOrganic ChemistryGeneral ChemistryOligosaccharideResorcinareneKineticschemistryGasesCalixarenesIon cyclotron resonanceChemistry - A European Journal
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Combined effect of the DeltaPhe or DeltaAla residue and the p-nitroanilide group on a didehydropeptides conformation.

2007

Two series of dehydropeptides of the general formulae Boc-Gly-X-Phe-p-NA, Boc-Gly-Gly-X-Phe-p-NA, Gly-X-Gly-Phe-p-NA·TFA, and Boc-Gly-X-Gly-Phe-p-NA, with X = ΔZPhe and ΔAla, were studied with NMR in DMSO and CDCl3-DMSO, and with CD in MeOH, MeCN, and TFE. The NMR spectra measured in DMSO suggest that peptides with the ΔPhe residue next to Phe are folded whereas peptides with Gly between ΔPhe and Phe are less ordered. NMR spectra of ΔAla-containing peptides indicate that these peptides are flexible and their conformational equilibria are populated by many different conformations. The CD spectra show that conformational properties of the peptides studied are distinctly influenced by a mutual…

Models MolecularCircular dichroismanimal structuresMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineBiophysicsBiochemistryBiomaterialsResidue (chemistry)Spectroscopy Fourier Transform InfraredAlanineCrystallographyintegumentary systemChemistryMutual positionCircular DichroismOrganic ChemistryGeneral MedicineDipeptidesAmidesNMR spectra databaseSolventCrystallographyModels Chemicalembryonic structuresX-ray crystallographyBiopolymers
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Effect of the ΔPhe residue configuration on a didehydropeptides conformation: A combined CD and NMR study.

2010

Conformations of two pairs of dehydropeptides with the opposite configuration of the ΔPhe residue, Boc-Gly-Δ(Z)Phe-Gly-Phe-OMe (Z-OMe), Boc-Gly-Δ(E)Phe-Gly-Phe-OMe (E-OMe), Boc-Gly-Δ(Z)Phe-Gly-Phe-p-NA (Z-p-NA), and Boc-Gly-Δ(E)Phe-Gly-Phe-p-NA (E-p-NA) were compared on the basis of CD and NMR studies in MeOH, trifluoroethanol (TFE), MeCN, chloroform, and dimethylsulfoxide (DMSO). The CD results were used as the additional input data for the NMR-based determination of the detailed solution conformations of the peptides. It was found that E-OMe is unordered and Z-OMe, Z-p-NA, and E-p-NA adopt the β-turn conformation. There are two overlapping β-turns in each of those peptides: type II and ty…

Models MolecularCircular dichroismanimal structuresdehydropeptide conformationMagnetic Resonance SpectroscopyStereochemistryProtein ConformationPhenylalanineBiophysicsStereoisomerismBiochemistrydehydrophenylalanine configurationBiomaterialschemistry.chemical_compoundResidue (chemistry)Protein structureotorhinolaryngologic diseasesMoleculeAmino Acid SequencePeptide sequenceChloroformintegumentary systemMolecular StructureCircular DichroismOrganic ChemistryTemperatureStereoisomerismGeneral MedicineNuclear magnetic resonance spectroscopySolutionsnuclear magnetic resonancedehydropeptideschemistrySpectrophotometryOligopeptidesBiopolymers
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Piperazine bridged resorcinarene cages.

2010

The one-pot Mannich condensation of resorcinarenes with piperazine and an excess of formaldehyde under high dilution conditions results in a helical cage, namely, a covalently linked dimer of two resorcinarenes connected via four piperazine bridges in yields ranging from 20 to 40%. The compounds were analyzed by NMR spectroscopy, ESI mass spectrometry, and single crystal X-ray diffraction. The helical cages can encapsulate small guest molecules by adapting the cavity volume by changing the helical pitch according to the guest size.

Models MolecularDimerPhenylalanineOrganic ChemistryFormaldehydeMolecular ConformationStereoisomerismNuclear magnetic resonance spectroscopyResorcinareneCrystallography X-RayBiochemistryPiperazineschemistry.chemical_compoundPiperazinechemistryCovalent bondPolymer chemistryMoleculeOrganic chemistryPhysical and Theoretical ChemistryCalixarenesSingle crystalPiperazineOrganic letters
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alpha 11beta 1 integrin recognizes the GFOGER sequence in interstitial collagens.

2002

The integrins alpha(1)beta(1), alpha(2)beta(1), alpha(10)beta(1), and alpha(11)beta(1) are referred to as a collagen receptor subgroup of the integrin family. Recently, both alpha(1)beta(1) and alpha(2)beta(1) integrins have been shown to recognize triple-helical GFOGER (where single letter amino acid nomenclature is used, O = hydroxyproline) or GFOGER-like motifs found in collagens, despite their distinct binding specificity for various collagen subtypes. In the present study we have investigated the mechanism whereby the latest member in the integrin family, alpha(11)beta(1), recognizes collagens using C2C12 cells transfected with alpha(11) cDNA and the bacterially expressed recombinant a…

Models MolecularIntegrinsDNA ComplementaryReceptors CollagenPhenylalanineIntegrinAmino Acid MotifsPlasma protein bindingBiochemistrylaw.inventionCollagen receptorMiceProtein structurelawCell AdhesionAnimalsHumansMagnesiumMolecular BiologyBinding selectivityCells Culturedchemistry.chemical_classificationbiologyDose-Response Relationship DrugCell BiologyPrecipitin TestsRecombinant ProteinsAmino acidProtein Structure TertiaryKineticschemistryBiochemistrybiology.proteinRecombinant DNACalciumCollagenPeptidesType I collagenProtein BindingThe Journal of biological chemistry
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Synthesis and structure of mono-bridged resorcinarene host: a ditopic receptor for ammonium guests.

2009

The synthesis and structural properties of tetramethoxy resorcinarene mono-crown-5 (1) are described. The binding characteristics of 1 toward acetylcholine and tetramethylammonium salts were investigated by 1H NMR titration. It was observed that the cavity of 1 provides a better fit to acetylcholine compared to the smaller tetramethylammonium cation, as acetylcholine is able to interact with both the crown ether moiety and the free hydroxyl groups of receptor 1 simultaneously.

Models MolecularMagnetic Resonance SpectroscopyStereochemistryPhenylalanineMolecular ConformationBiochemistrychemistry.chemical_compoundPolymer chemistrymedicineHydroxidesMoietyPhysical and Theoretical ChemistryCrown etherchemistry.chemical_classificationTetramethylammoniumBinding SitesOrganic ChemistryNuclear magnetic resonance spectroscopyResorcinareneCrown CompoundsQuaternary Ammonium CompoundschemistryProton NMRTitrationCalixarenesAcetylcholinemedicine.drugOrganicbiomolecular chemistry
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Mapping the tRNA binding site on the surface of human DNMT2 methyltransferase.

2012

The DNMT2 enzyme methylates tRNA-Asp at position C38. Because there is no tRNA–Dnmt2 cocrystal structure available, we have mapped the tRNA binding site of DNMT2 by systematically mutating surface-exposed lysine and arginine residues to alanine and studying the tRNA methylation activity and binding of the corresponding variants. After mutating 20 lysine and arginine residues, we identified eight of them that caused large (>4-fold) decreases in catalytic activity. These residues cluster within and next to a surface cleft in the protein, which is large enough to accommodate the tRNA anticodon loop and stem. This cleft is located next to the binding pocket for the cofactor S-adenosyl-l-methion…

Models MolecularMethyltransferaseProtein ConformationLysineMolecular Sequence DataBiologyBiochemistryMethylationCofactorRNA TransferAnimalsHumansAmino Acid SequenceDNA (Cytosine-5-)-MethyltransferasesCloning MolecularAlaninechemistry.chemical_classificationTRNA methylationBinding SitesCircular DichroismTRNA bindingEnzymeDrosophila melanogasterchemistryBiochemistryAmino Acid SubstitutionTransfer RNAbiology.proteinMutagenesis Site-DirectedNucleic Acid ConformationSequence AlignmentBiochemistry
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