Search results for "Kinetics"

showing 10 items of 2224 documents

Conformational changes involved in thermal aggregation processes of bovine serum albumin

2003

We report a kinetic study on thermal aggregation process of the model protein bovine serum albumin (BSA) in low concentration regime. Aim of this study is to provide information on relationship between conformational changes and initial step of aggregation. The experimental approach is based on steady-state fluorescence spectra of the two tryptophans located in two different domains, in way to study conformational changes in the surrounding of these residues. We also follow emission spectra of Fluorescein-5-Maleimide dye bound to the single free cysteine of BSA. Complementary information on the extent of aggregation and on the structural changes is obtained by Rayleigh scattering and circul…

Protein DenaturationCircular dichroismHot TemperatureLightKineticsSerum albuminBiophysicsProtein aggregationCircular dichroismBiochemistryProtein Structure SecondaryProtein structureAnimalsHumansScattering RadiationCysteineBovine serum albuminPhysical and Theoretical ChemistryProtein secondary structurebiologyChemistryOrganic ChemistryTryptophanSerum Albumin BovineFluoresceinsConformational changeProtein Structure TertiaryKineticsCrystallographySpectrometry FluorescenceBovine serum albuminSteady-state fluorescencebiology.proteinCattlesense organsProtein aggregationCysteine
researchProduct

Thermal aggregation of beta-lactoglobulin in presence of metal ions.

2007

In this work, we report a study of the effects of zinc and copper ions on the heat-induced aggregation of beta-lactoglobulin (BLG). Kinetics investigations on aggregates growth by light scattering measurements and on secondary structure changes by FTIR absorption measurements show the different role played by the two metals during the whole process. In particular, the presence of zinc in solution promotes the formation of aggregates of BLG at a lower temperature than copper. Then, at fixed temperature, formation of a large amount of aggregates, of large dimension, is observed for Zn-BLG in shorter time; on the contrary, the presence of copper in solution does not affect the aggregation proc…

Protein DenaturationHot TemperatureCations DivalentMetal ions in aqueous solutionKineticsInorganic chemistryBiophysicsBeta-lactoglobulinchemistry.chemical_elementZincLactoglobulinsProtein aggregationBiochemistryProtein Structure SecondaryDivalentSpectroscopy Fourier Transform InfraredAnimalsMetal ionProtein secondary structurechemistry.chemical_classificationOrganic ChemistryLight scatteringCopperSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)FTIR spectroscopyKineticsZincchemistryChemical engineeringCattleAbsorption (chemistry)Protein aggregationCopperBiophysical chemistry
researchProduct

Inhibition of prolyl hydroxylation and procollagen processing in chick-embryo calvaria by a derivative of pyridine-2,4-dicarboxylate. Characterizatio…

1991

The biochemical and morphological consequences of procollagen prolyl 4-hydroxylase inhibition by pyridine-2,4-dicarboxylic acid (2,4-PDCA) and its diethyl ester (diethyl-2,4-PDC) were studied in chick-embryo calvaria, which predominantly synthesize type I collagen. Half-maximal inhibition of tissue hydroxyproline formation required 650 microM-2,4-PDCA, whereas the Ki with respect to chicken prolyl 4-hydroxylase in vitro was 2 microM. In contrast, half-maximal inhibition was caused by 10 microM-diethyl-2,4-PDC in the intact calvaria, although chicken prolyl 4-hydroxylase in vitro was not inhibited even at 1 mM. The collagenous material produced in the presence of diethyl-2,4-PDC showed an al…

Protein DenaturationProtein ConformationPyridinesProcollagen-Proline DioxygenaseCalvariaChick EmbryoEndoplasmic ReticulumModels BiologicalBiochemistryBone and BonesHydroxylationHydroxyprolinechemistry.chemical_compoundmedicineAnimalsMolecular BiologyCells CulturedEndoplasmic reticulumCell BiologyIn vitroKineticsProcollagen peptidasemedicine.anatomical_structurechemistryBiochemistryMicrosomeCollagenProcollagenType I collagenResearch ArticleBiochemical Journal
researchProduct

Single Unlabeled Protein Detection on Individual Plasmonic Nanoparticles

2012

The ultimate detection limit in analytic chemistry and biology is the single molecule. Commonly, fluorescent dye labels or enzymatic amplification are employed. This requires additional labeling of the analyte, which modifies the species under investigation and therefore influences biological processes. Here, we utilize single gold nanoparticles to detect single unlabeled proteins with extremely high temporal resolution. This allows for monitoring the dynamic evolution of a single protein binding event on a millisecond time scale. The technique even resolves equilibrium coverage fluctuations, opening a window into Brownian dynamics of unlabeled macromolecules. Therefore, our method enables …

Protein FoldingAnalyteSurface PropertiesMetal NanoparticlesBioengineeringNanotechnology02 engineering and technology010402 general chemistry01 natural sciencesNanotechnologyGeneral Materials ScienceSoft matterSurface plasmon resonancePlasmonic nanoparticlesChemistryMechanical EngineeringProteinsGeneral ChemistrySurface Plasmon Resonance021001 nanoscience & nanotechnologyCondensed Matter Physics0104 chemical sciencesKineticsBrownian dynamicsProtein foldingAdsorptionGold0210 nano-technologyBiological systemMacromoleculeProtein adsorptionNano Letters
researchProduct

The membrane proximal cytokine receptor domain of the human interleukin-6 receptor is sufficient for ligand binding but not for gp130 association.

1998

Interleukin-6 (IL-6) belongs to the family of the "four-helix bundle" cytokines. The extracellular parts of their receptors consist of several Ig- and fibronectin type III-like domains. Characteristic of these receptors is a cytokine-binding module consisting of two such fibronectin domains defined by a set of four conserved cysteines and a tryptophan-serine-X-tryptophan-serine (WSXWS) sequence motif. On target cells, IL-6 binds to a specific IL-6 receptor (IL-6R), and the complex of IL-6.IL-6R associates with the signal transducing protein gp130. The IL-6R consists of three extracellular domains. The NH2-terminal Ig-like domain is not needed for ligand binding and signal initiation. Here w…

Protein FoldingProtein ConformationEnzyme-Linked Immunosorbent AssayPlasma protein bindingImmunoglobulin domainBiologyLigandsBiochemistryHAMP domainAntigens CDCytokine Receptor gp130HumansMolecular BiologyDNA PrimersMembrane GlycoproteinsBase SequenceInterleukin-6Cell BiologyHydrogen-Ion ConcentrationGlycoprotein 130Precipitin TestsReceptors Interleukin-6Recombinant ProteinsCell biologyKineticsBiochemistryMATH domainSignal transductionCytokine receptorBinding domainProtein BindingSignal TransductionThe Journal of biological chemistry
researchProduct

Template-Directed Protein Folding into a Metastable State of Increased Activity

1995

The principal objective of this work was to distinguish between kinetic and thermodynamic reaction control in protein folding. The deleterious effects of a specific mutation on spontaneous refolding competence were analyzed for this purpose. A Bowman-Birk-type proteinase inhibitor of trypsin and chymotrypsin was selected as a double-headed model protein to facilitate the detection of functional irregularities by the use of functional assays. The parent protein spontaneously folds into a single, fully active and thermodynamically stable state in a redox buffer after reduction/denaturation. By contrast, the properties of a P'1Ser--Pro variant in the trypsin-reactive subdomain differ before an…

Protein FoldingProtein ConformationMolecular Sequence DataPopulationDNA RecombinantPhi value analysisBiochemistryDenaturation (biochemistry)Amino Acid SequenceeducationConformational isomerismTrypsin Inhibitor Bowman-Birk Soybeaneducation.field_of_studyChymotrypsinBase SequencebiologyChemistryGenetic VariationContact orderSolutionsKineticsCrystallographyModels Chemicalbiology.proteinThermodynamicsProtein foldingDownhill foldingEuropean Journal of Biochemistry
researchProduct

Investigation of protein folding by coarse-grained molecular dynamics with the UNRES force field.

2010

Coarse-grained molecular dynamics simulations offer a dramatic extension of the time-scale of simulations compared to all-atom approaches. In this article, we describe the use of the physics-based united-residue (UNRES) force field, developed in our laboratory, in protein-structure simulations. We demonstrate that this force field offers about a 4000-times extension of the simulation time scale; this feature arises both from averaging out the fast-moving degrees of freedom and reduction of the cost of energy and force calculations compared to all-atom approaches with explicit solvent. With massively parallel computers, microsecond folding simulation times of proteins containing about 1000 r…

Protein FoldingStaphylococcus aureusRotationMolecular Dynamics SimulationKinetic energyForce field (chemistry)Protein Structure SecondaryArticleMolecular dynamicsMiceProtein structureBacterial ProteinsComputational chemistryAnimalsStatistical physicsPhysical and Theoretical ChemistryMassively parallelQuantitative Biology::BiomoleculesPrincipal Component AnalysisModels StatisticalChemistryProteinsMicrosecondKineticsBundleSolventsThermodynamicsProtein foldingTranscriptional Elongation FactorsCarrier ProteinsAlgorithmsProtein BindingThe journal of physical chemistry. A
researchProduct

The Metalloprotease Meprin β Generates Amino Terminal-truncated Amyloid β Peptide Species

2012

The amyloid β (Aβ) peptide, which is abundantly found in the brains of patients suffering from Alzheimer disease, is central in the pathogenesis of this disease. Therefore, to understand the processing of the amyloid precursor protein (APP) is of critical importance. Recently, we demonstrated that the metalloprotease meprin β cleaves APP and liberates soluble N-terminal APP (N-APP) fragments. In this work, we present evidence that meprin β can also process APP in a manner reminiscent of β-secretase. We identified cleavage sites of meprin β in the amyloid β sequence of the wild type and Swedish mutant of APP at positions p1 and p2, thereby generating Aβ variants starting at the first or seco…

ProteomicsMolecular Sequence DataMutantPeptideBiologyHydroxamic AcidsCleavage (embryo)BiochemistryCatalysis03 medical and health sciences0302 clinical medicineAlzheimer Diseasemental disordersmedicineAmyloid precursor proteinHumansProtein IsoformsAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMetalloproteinaseAmyloid beta-PeptidesWild typeBrainMetalloendopeptidasesMolecular Bases of DiseaseCell Biologymedicine.diseaseMolecular biologyProtein Structure TertiaryKineticsHEK293 CellsEnzymechemistryBiochemistryMutationMetalloproteasesbiology.proteinAmyloid Precursor Protein SecretasesAlzheimer's diseasePeptides030217 neurology & neurosurgeryJournal of Biological Chemistry
researchProduct

Mechanism of aminocarbene formation by nucleophilic attack on isocyanide ligands in platinum(II)2-pyrazyl and 4-pyridyl complexes

1997

Abstract The reactions of 2-pyrazyl and 4-pyridyl isocyanide complexes [Pt(CNC 6 H 11 )(C 4 H 3 N 2 - C 2 )(dppe)ClO 4 and [Pt(CNC 6 H 11 )(C 5 H 4 N- C 4 ) (dppe)]ClO 4 ( 1 ) with amines involving the formation of aminocarbene derivatives have been studied kinetically in 1,2-dichloroethane by UV—VIS techniques. The kinetics obey the simple second-order rate law rate = k 2 [ 1 ][amine]. Low activation enthalpies and highly negative activation entropies for the k 2 term are observed. A mechanism is proposed involving direct nucleophilic attack of the amine on the isocyanide carbon with concomitant proton transfer from the amine to the isocyanide nitrogen assisted by the heterocyclic nitrogen…

ProtonChemistryLigandIsocyanideOrganic ChemistryKineticschemistry.chemical_elementPhotochemistryBiochemistryMedicinal chemistryNitrogenInorganic Chemistrychemistry.chemical_compoundNucleophileMaterials ChemistryAmine gas treatingPhysical and Theoretical ChemistryPlatinum
researchProduct

D-Malic enzyme of Pseudomonas fluorescens.

1982

By the enrichment culture technique 14 gram-negative bacteria and two yeast strains were isolated that used D(+)-malic acid as sole carbon source. The bacteria were identified as Pseudomonas putida, Pseudomonas fluorescens, Pseudomonas aeruginosa and Klebsiella aerogenes. In cell-free extracts of P. fluorescens and P. putida the presence of malate dehydrogenase, D-malic enzyme (NAD-dependent) and L-malic enzyme (NADP-dependent) was demonstrated. D-Malic enzyme from P. fluorescens was purified. Stabilization of the enzyme by 50 mM ammonium sulphate an 1 mM EDTA was essential. Preparation of D-malic enzyme that gave one band with disc gel electrophoresis showed a specific activity of 4-5 U/mg…

Pseudomonas fluorescensEnterobacter aerogenesPseudomonas fluorescensBiochemistryMalate dehydrogenasechemistry.chemical_compoundMalate DehydrogenaseOxaloacetic acidPseudomonasPolyacrylamide gel electrophoresischemistry.chemical_classificationGel electrophoresisChromatographybiologyCell-Free Systemfungifood and beveragesbiology.organism_classificationPseudomonas putidaMolecular WeightKineticsKlebsiella pneumoniaeEnzymechemistryBiochemistryElectrophoresis Polyacrylamide GelEuropean journal of biochemistry
researchProduct