Search results for "Conformational change"

showing 10 items of 69 documents

Impact of Pulsed Electric Fields on Enzymes

2017

International audience; Pulsed electric field (PEF) processing has emerged as a promising technology in the development of tailor-made processes to effectively control the enzyme activity. It has been proven as an effective technique for the preservation of food products as it can result in substantial inactivation of most undesirable enzymes. When compared to microbial inactivation, however, large specific energy inputs are required to inactivate enzymes. The existing evidence suggests that PEF can also stimulate the activity of beneficial enzymes at low intense treatments. The PEF affects enzyme activity by changing mainly the secondary (α-helix, β-sheets, etc.), tertiary (spatial conform…

Conformational changes0301 basic medicineProteasesFood processing[SDV.BIO]Life Sciences [q-bio]/Biotechnology[SDV]Life Sciences [q-bio]010402 general chemistry01 natural sciencesPolyphenol oxidase03 medical and health sciences[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringEnzyme activityLipasePulsed electric fieldchemistry.chemical_classificationbiologyChemistryEnzyme structureEnzyme assayEnzymesrespiratory tract diseases0104 chemical sciences030104 developmental biologyEnzymeBiochemistrybiology.proteinAlkaline phosphatase[SDV.AEN]Life Sciences [q-bio]/Food and NutritionPeroxidase
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Identification and cloning of odorant binding proteins from the scarab beetle Phyllopertha diversa.

1999

Abstract Wehave identified, cloned, and characterized two odorant binding proteins from the pale brown chafer, Phyllopertha diversa. One of the proteins (OBP1, 116 amino acids long) showed high amino acid identity (>90%) to two previously identified PBPs from scarab beetles. The second protein (OBP2) showed limited sequence similarity to lepidopteran and dipteran OBPs, but contained only 133 amino acids. Both proteins showed the occurrence of six highly conserved cysteines; electrospray mass spectral data suggested they are all bound in three disulfide bonds. During purification, OBP2 separated into several isoforms; N-terminal amino acid sequencing and electrospray ionization mass spectrom…

Gene isoformOdorant bindingElectrospray ionization1Molecular Sequence DataBiophysicsPhyllopertha diversaReceptors Odorantelectrospray mass spectrometryBiochemistryBombykolbombykolpheromonechemistry.chemical_compoundconformational changeBombyx moriAnimalsAmino Acid SequenceCloning MolecularMolecular Biologychemistry.chemical_classificationCloningbiologySequence Homology Amino Acid3H)-quinazolinedionefungi3-dimethyl-2Cell Biologybiology.organism_classificationRecombinant ProteinsjaponilureAmino acidColeopteraMolecular WeightchemistryBiochemistryOdorantsPheromone4-(1HSequence AlignmentBiochemical and biophysical research communications
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Polymer dynamics in thin p-type conducting films investigated by ac-electrogravimetry. Kinetics aspects on anion exclusion, free solvent transfer, an…

2015

A new transfer model is proposed to explain ac-electrogravimetry response of p-doped films. This model takes into account the exclusion effect occurring as a result of the anion transfer. The insertion/expulsion of anions inside a film involves simultaneously the expulsion/insertion of free solvent molecules. The number of solvent molecules excluded depends on the volume of anion transferred. Solvent transfer stimulated by the conformational changes of films constitutes the remaining electrogravimetric response when the exclusion process cannot explain by itself this response. Consequently, the kinetics of this free solvent transfer can be directly related to the kinetics of conformational …

General Chemical EngineeringKineticsElectrochemical kinetics02 engineering and technology010402 general chemistryPhotochemistryElectrochemistry01 natural scienceselectrochemical quartz crystal microbalanceElectrogravimetryPolymer chemistryElectrochemistryMolecule[CHIM]Chemical Sciencesconformational changeschemistry.chemical_classificationConductive polymerPolymer021001 nanoscience & nanotechnology0104 chemical sciencesSolventelectrochemical impedance spectroscopychemistryIntrinsically conducting polymer0210 nano-technology[CHIM.OTHE]Chemical Sciences/Other
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The Halide Binding Behavior of 2-Carbamoyl-7-ureido-1H-indoles: Conformational Aspects

2009

Indole-based anion receptors with an carboxamide unit in 2- and an urea in 7-position were prepared and found to bind halides (as well as acetate and nitrate) in chloroform solutions at room temperature. Investigations of the binding behaviour show that the receptor is selective for chloride. Surprisingly, the truncated receptor 3 without the 2-carbamoyl substituent shows the highest affinity for Cl–. Thorough 1H, 13C and 15N NMR investigations indicate different binding modes for acetate, nitrate and halides to the receptor 2. The observation of a major conformational change of this receptor during the binding of the halide ions leads to an understanding of the relative binding affinities …

Indole testConformational changeHydrogen bondmedicine.drug_classStereochemistryOrganic ChemistryQuinolineSubstituentHalideCarboxamideNuclear magnetic resonance spectroscopychemistry.chemical_compoundchemistrymedicinePhysical and Theoretical ChemistryEuropean Journal of Organic Chemistry
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Conformational Change in the Pheromone-binding Protein fromBombyx mori Induced by pH and by Interaction with Membranes

1999

The pheromone-binding protein (PBP) from Bombyx mori was expressed in Escherichia coli periplasm. It specifically bound radiolabeled bombykol, the natural pheromone for this species. It appeared as a single band both in native and SDS-polyacrylamide gel electrophoresis and was also homogeneous in most chromatographic systems. However, in ion-exchange chromatography, multiple forms sometimes appeared. Attempts to separate them revealed that they could be converted into one another. Analysis of the protein by circular dichroism and fluorescence spectroscopy demonstrated that its tertiary structure was sensitive to pH changes and that a dramatic conformational transition occurred between pH 6.…

MaleConformational changeCircular dichroismSensory Receptor CellsProtein ConformationBiochemistryBombykolchemistry.chemical_compoundEscherichia coliAnimalsDenaturation (biochemistry)Pheromone bindingCloning MolecularMolecular BiologyChemistryCircular DichroismCell BiologyHydrogen-Ion ConcentrationBombyxChromatography Ion ExchangeLigand (biochemistry)Protein tertiary structureProtein Structure TertiarySpectrometry FluorescenceBiochemistryBiophysicsInsect ProteinsIntercellular Signaling Peptides and ProteinsThermodynamicsElectrophoresis Polyacrylamide GelCarrier ProteinsPheromone binding proteinJournal of Biological Chemistry
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Electrochemically induced free solvent transfer in thin poly(3,4-ethylenedioxythiophene) films

2015

International audience; In dynamic intrinsically conducting films, counterions transfer and conformational movements stimulated by the electrochemical reactions affect the free water molecules transfer. Poly(3,4-ethylenedioxythiophene) or PEDOT is included in this category. Here, p-doping of PEDOT immersed in LiClO4 aqueous solution was explored by ac-electrogravimetry. Electrochemical impedance spectroscopy combined with mass impedance spectroscopy proves useful for species identification and kinetics. For PEDOT, new equations have been developed to analyze the ac -electrogravimetry response. Quantitatively, faster free water transfer and slower coupled View the MathML sourceClO4−/free wat…

Materials scienceGeneral Chemical EngineeringAnalytical chemistry02 engineering and technology010402 general chemistryElectrochemistry01 natural scienceschemistry.chemical_compoundPEDOT:PSSac-ElectrogravimetryElectrochemistryMoleculeElectrochemical quartz crystal microbalance[CHIM]Chemical SciencesElectrochemically induced conformational changeschemistry.chemical_classificationAqueous solutionPolymerPoly(3021001 nanoscience & nanotechnology0104 chemical sciencesDielectric spectroscopychemistryChemical engineeringCounterion4-ethylenedioxythiophene)0210 nano-technology[CHIM.OTHE]Chemical Sciences/OtherElectrochemical impedance spectroscopyPoly(34-ethylenedioxythiophene)
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Tracking the structural dynamics of proteins in solution using time-resolved wide-angle X-ray scattering

2008

We demonstrate tracking of protein structural changes with time-resolved wide-angle X-ray scattering (TR-WAXS) with nanosecond time resolution. We investigated the tertiary and quaternary conformational changes of human hemoglobin under nearly physiological conditions triggered by laser-induced ligand photolysis. We also report data on optically induced tertiary relaxations of myoglobin and refolding of cytochrome c to illustrate the wide applicability of the technique. By providing insights into the structural dynamics of proteins functioning in their natural environment, TR-WAXS complements and extends results obtained with time-resolved optical spectroscopy and X-ray crystallography.

Materials scienceProtein ConformationCrystallography X-RayBiochemistrySensitivity and SpecificityArticlechemistry.chemical_compoundHemoglobinsProtein structureScattering RadiationSpectroscopyWide-angle X-ray scatteringMolecular Biologyprotein dynamics conformational changes hemoglobin myoglobin cytochrome cScatteringMyoglobinX-RaysResolution (electron density)Cytochromes cCell BiologyNanosecondMyoglobinchemistryChemical physicsProtein quaternary structuresense organsBiotechnology
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Probing in cell protein structural changes with time-resolved X-ray scattering

2012

International audience; Investigating protein structural changes inside the cell is a major goal in molecular biology. Here we show that time-resolved wide-angle X-ray scattering is a valuable tool for this purpose. Hemoglobin has been chosen as a model system and its tertiary and quaternary conformational changes following laser flash-photolysis have been tracked in intact red blood cells with nanosecond time resolution.

Model system010402 general chemistry01 natural scienceslaw.invention03 medical and health scienceslaw030304 developmental biology0303 health sciencesChemistryScatteringX-rayTime resolutionin cell studieGeneral ChemistryNanosecondX-ray scatteringCondensed Matter PhysicsLaserConformational changeSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical sciencesCrystallographyChemical physicsAllosteric transitionProtein dynamicsense organs[PHYS.COND.CM-SCM]Physics [physics]/Condensed Matter [cond-mat]/Soft Condensed Matter [cond-mat.soft]
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Electrostatic Tuning of the Ligand Binding Mechanism by Glu27 in Nitrophorin 7

2018

AbstractNitrophorins (NP) 1–7 are NO-carrying heme proteins found in the saliva of the blood-sucking insect Rhodnius prolixus. The isoform NP7 displays peculiar properties, such as an abnormally high isoelectric point, the ability to bind negatively charged membranes, and a strong pH sensitivity of NO affinity. A unique trait of NP7 is the presence of Glu in position 27, which is occupied by Val in other NPs. Glu27 appears to be important for tuning the heme properties, but its influence on the pH-dependent NO release mechanism, which is assisted by a conformational change in the AB loop, remains unexplored. Here, in order to gain insight into the functional role of Glu27, we examine the ef…

Models Molecular0301 basic medicineConformational changeProtein ConformationMolecular biologylcsh:MedicineSangCrystallography X-RayLigands01 natural scienceschemistry.chemical_compoundProtein structureModelsZoologiaBloodsucking insectsNitrophorinStatic electricitylcsh:ScienceHemeCell receptorschemistry.chemical_classificationCrystallographyMultidisciplinaryParasitologiaAmino acidBloodRhodniusInsect ProteinsAnimals; Crystallography X-Ray; Glutamic Acid; Heme; Hemeproteins; Insect Proteins; Ligands; Models Molecular; Molecular Dynamics Simulation; Mutation; Protein Conformation; Rhodnius; Salivary Proteins and Peptides; Static ElectricityHemeproteinsHemeproteinStatic ElectricityGlutamic AcidHemeMolecular Dynamics Simulation010402 general chemistryArticle03 medical and health sciencesAnimalsSalivary Proteins and PeptidesBiologia molecularInsectes hematòfags030102 biochemistry & molecular biologylcsh:RMolecular0104 chemical sciencesIsoelectric pointchemistryMutationX-RayBiophysicslcsh:QReceptors cel·lularsParasitologyZoologyScientific Reports
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The route to protein aggregate superstructures: Particulates and amyloid-like spherulites.

2015

AbstractDepending on external conditions, native proteins may change their structure and undergo different association routes leading to a large scale polymorphism of the aggregates. This feature has been widely observed but is not fully understood yet. This review focuses on morphologies, physico-chemical properties and mechanisms of formation of amyloid structures and protein superstructures. In particular, the main focus will be on protein particulates and amyloid-like spherulites, briefly summarizing possible experimental methods of analysis. Moreover, we will highlight the role of protein conformational changes and dominant forces in driving association together with their connection w…

Models MolecularAmyloidAmyloid Superstructures Protein aggregation spectroscopyProtein superstructureProtein ConformationBiophysicsNanotechnologyProtein aggregationProtein particulateBiochemistryProtein Aggregation PathologicalProtein AggregatesX-Ray DiffractionStructural BiologyElectrostaticsGeneticsHumansMolecular BiologyAmyloid likeAmyloid-like spheruliteChemistryCell BiologyConformational changeSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Microscopy Fluorescence MultiphotonModels ChemicalAggregate structureThermodynamicsExperimental methodsProtein aggregationFEBS letters
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