Search results for "kinetics"

showing 10 items of 2224 documents

Internal dynamics and protein-matrix coupling in trehalose-coated proteins.

2005

Abstract We review recent studies on the role played by non-liquid, water-containing matrices on the dynamics and structure of embedded proteins. Two proteins were studied, in water–trehalose matrices: a water-soluble protein (carboxy derivative of horse heart myoglobin) and a membrane protein (reaction centre from Rhodobacter sphaeroides ). Several experimental techniques were used: Mossbauer spectroscopy, elastic neutron scattering, FTIR spectroscopy, CO recombination after flash photolysis in carboxy-myoglobin, kinetic optical absorption spectroscopy following pulsed and continuous photoexcitation in Q B containing or Q B deprived reaction centre from R. sphaeroides . Experimental result…

Models MolecularAbsorption spectroscopyPhotosynthetic Reaction Center Complex ProteinsBiophysicsHemeRhodobacter sphaeroidesNeutron scatteringBiochemistryAnalytical Chemistrychemistry.chemical_compoundRhodobacter sphaeroidesMolecular dynamicsSpectroscopy Fourier Transform InfraredComputer SimulationMolecular Biologytrehalose protein simulation spectroscopyPhotolysisbiologyHydrogen bondMyoglobinTemperatureTrehaloseWaterHydrogen Bondingbiology.organism_classificationCrystallographyKineticsMyoglobinchemistryMembrane proteinFlash photolysisBiochimica et biophysica acta
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Hemocyanin from E. californicum encapsulated in silica gels: oxygen binding and conformational states.

2007

Cooperativity depends on the existence of equilibria among functionally distinct conformational states that are affected by homo and heterotropic effectors. In order to isolate the quaternary conformations of hemocyanin from E. californicum, the 24-meric giant protein was encapsulated in wet, nanoporous silica gels, either in the absence or presence of oxygen. The deoxy- and oxy-hemocyanin gels exhibit a p50 for oxygen of 11 and 2.5 torr, respectively, values in close agreement with those for hemocyanin in solution. The observed Hill coefficients are lower than unity, indicating a conformational heterogeneity within each locked conformational state, a finding in agreement with the assumptio…

Models MolecularAbsorption spectroscopyProtein Conformationmedicine.medical_treatmentchemistry.chemical_elementCooperativityBiologyOxygenGeneticsmedicineAnimalsNanoporousHemocyaninSpidersGeneral MedicineSilicon DioxideOxygenSolutionsCrystallographyKineticsBiochemistrychemistrySpectrophotometryHemocyaninsHemoglobinGelsOxygen bindingAlgorithmsProtein BindingGene
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Polymeric prodrug for release of an antitumoral agent by specific enzymes.

2001

The clinical usefulness of antitumor chemotherapy has been strongly limited by the lack of specificity of most anticancer drugs, which act also against healthy cells. The aim of this work was to design, synthesize, and evaluate a macromolecular prodrug of Cytarabine, a known antitumor drug, which is a specific substrate for plasmin enzyme whose concentration is high in various kinds of tumor mass as a result of plasminogen activator secretion. alpha,beta-Poly(N-hydroxyethyl)-DL-aspartamide (PHEA), a known synthetic and biocompatible polyamino acid, was used as a drug carrier, and Cytarabine was linked to PHEA by D-Val-Leu-Lys spacer synthesized beginning from Cbz-D-Val-LeuOH dipeptide and N…

Models MolecularAntimetabolites AntineoplasticPlasminBiomedical EngineeringPharmaceutical ScienceBioengineeringchemistry.chemical_compoundPlasmaDrug StabilitymedicineHumansProdrugsFibrinolysinPharmacologychemistry.chemical_classificationDrug CarriersDipeptideChemistryOrganic ChemistryCytarabineIn vitroKineticsEnzymeBiochemistryDrug DesignCytarabineDrug carrierPeptidesPlasminogen activatorOligopeptidesBiotechnologymedicine.drugConjugateBioconjugate chemistry
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Elucidation of Pathways for NO Electroreduction on Pt(111) from First Principles

2015

The mechanism of nitric oxide electroreduction on Pt(111) is investigated using a combination of first principles calculations and electrokinetic rate theories. Barriers for chemical cleavage of N-O bonds on Pt(111) are found to be inaccessibly high at room temperature, implying that explicit electrochemical steps, along with the aqueous environment, play important roles in the experimentally observed formation of ammonia. Use of explicit water models, and associated determination of potential-dependent barriers based on Bulter-Volmer kinetics, demonstrate that ammonia is produced through a series of water-assisted protonation and bond dissociation steps at modest voltages (0.3 V). In addit…

Models MolecularAqueous solutionnitrous oxideChemistryKineticsProtonationGeneral MedicineGeneral ChemistryNitric OxideElectrocatalystElectrochemistryPhotochemistrychemistryammoniaCatalysisDissociation (chemistry)Ammoniachemistry.chemical_compoundelectrocatalysisDensity functional theoryta116NO reductiondensity functional theoryPlatinumAngewandte Chemie International Edition
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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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Design and construction of highly stable, protease-resistant chimeric avidins.

2005

The chicken avidin gene family consists of avidin and seven separate avidin-related genes (AVRs) 1-7. Avidin protein is a widely used biochemical tool, whereas the other family members have only recently been produced as recombinant proteins and characterized. In our previous study, AVR4 was found to be the most stable biotin binding protein thus far characterized (T(m) = 106.4 degrees C). In this study, we studied further the biotin-binding properties of AVR4. A decrease in the energy barrier between the biotin-bound and unbound state of AVR4 was observed when compared with that of avidin. The high resolution structure of AVR4 facilitated comparison of the structural details of avidin and …

Models MolecularBiotin bindingInsectaProtein familyProtein subunitRecombinant Fusion ProteinsMolecular Sequence DataBiotinBiosensing TechniquesBiologyProtein EngineeringBiochemistryProtein Structure SecondaryProtein structureAnimalsAmino Acid SequenceMolecular BiologyThermostabilityCalorimetry Differential ScanningSequence Homology Amino AcidTemperatureCell BiologyProtein engineeringAvidinRecombinant ProteinsProtein Structure TertiaryKineticsBiochemistryMicroscopy FluorescenceMutagenesisBiotinylationMutationbiology.proteinChromatography GelThermodynamicsElectrophoresis Polyacrylamide GelEndopeptidase KBaculoviridaeChickensAvidinChromatography LiquidPeptide HydrolasesProtein BindingThe Journal of biological chemistry
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Construction of a dual chain pseudotetrameric chicken avidin by combining two circularly permuted avidins.

2004

Two distinct circularly permuted forms of chicken avidin were designed with the aim of constructing a fusion avidin containing two biotin-binding sites in one polypeptide. The old N and C termini of wild-type avidin were connected to each other via a glycine/serine-rich linker, and the new termini were introduced into two different loops. This enabled the creation of the desired fusion construct using a short linker peptide between the two different circularly permuted subunits. The circularly permuted avidins (circularly permuted avidin 5 → 4 and circularly permuted avidin 6 → 5) and their fusion, pseudotetrameric dual chain avidin, were biologically active, i.e. showed biotin binding, and…

Models MolecularBiotin bindingProtein DenaturationProtein FoldingStereochemistryProtein ConformationProtein subunitMolecular Sequence DataGlycineBiotinBiochemistrySensitivity and SpecificityProtein Structure Secondarystomatognathic systemChain (algebraic topology)SerineAnimalsAmino Acid SequenceBinding siteProtein Structure QuaternaryMolecular BiologyLinker peptideBinding SitesbiologyCell Biologyrespiratory systemAvidinProtein Structure TertiaryCrystallographyKineticsMutationbiology.proteinChromatography GelElectrophoresis Polyacrylamide GelEndopeptidase KPeptidesLinkerChickensAvidinProtein BindingThe Journal of biological chemistry
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Pores Formed by Baxα5 Relax to a Smaller Size and Keep at Equilibrium

2010

AbstractPores made by amphipathic cationic peptides (e.g., antimicrobials and fragments of pore-forming proteins) are typically studied by examining the kinetics of vesicle leakage after peptide addition or obtaining structural measurements in reconstituted peptide-lipid systems. In the first case, the pores have been considered transient phenomena that allow the relaxation of the peptide-membrane system. In the second, they correspond to equilibrium structures at minimum free energy. Here we reconcile both approaches by investigating the pore activity of the α5 fragment from the proapoptotic protein Bax (Baxα5) before and after equilibrium of peptide/vesicle complexes. Quenching assays on …

Models MolecularCardiolipinsMacromolecular SubstancesKineticsMolecular Sequence DataBiophysicsPeptideIn Vitro TechniquesBiophysical PhenomenaAmphiphileAnimalsHumansAmino Acid SequencePeptide sequenceUnilamellar LiposomesFluorescent Dyesbcl-2-Associated X Proteinchemistry.chemical_classificationMicroscopy ConfocalChemistryBilayerVesicleMacromolecular SubstancesCationic polymerizationMembranePeptide FragmentsCrystallographyKineticsBiophysicsPhosphatidylcholinesThermodynamicsCattle
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The solution behavior of dopamine in the presence of mono and divalent cations: A thermodynamic investigation in different experimental conditions

2021

The interactions of dopamine [2-(3,4-Dihydroxyphenyl)ethylamine, (Dop-)] with methylmercury(II) (CH3Hg+), magnesium(II), calcium(II), and tin(II) were studied in NaCl(aq) at different ionic strengths and temperatures. Different speciation models were obtained, mainly characterized by mononuclear species. Only for Sn2+ we observed the formation of binuclear complexes (M2L2 and M2LOH (charge omitted for simplicity)

Models MolecularCations DivalentDopaminePotentiometric titrationEnthalpyIonic bondingBiochemistryMicrobiologyArticleDivalentchemistry.chemical_compoundMetal complexesTheoryofComputation_ANALYSISOFALGORITHMSANDPROBLEMCOMPLEXITYSettore CHIM/01 - Chimica AnaliticaStability constantsMolecular Biologychemistry.chemical_classificationCatechol; Chemical speciation; Metal complexes; Sequestration; Stability constantsLigandHydrolysisOsmolar ConcentrationTemperatureSequestrationHydrogen-Ion ConcentrationQR1-502SolutionsKineticschemistrySpecific ion interaction theoryIonic strengthThermogravimetryCatecholPhysical chemistryThermodynamicsChemical speciationEthylamine
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