Search results for "denaturation"

showing 10 items of 107 documents

Modulation of DNA binding by reversible metal-controlled molecular reorganizations of scorpiand-like ligands.

2012

DNA interaction with scorpiand azamacrocycles has been achieved through modulation of their binding affinities. Studies performed with different experimental techniques provided evidence that pH or metal-driven molecular reorganizations of these ligands regulate their ability to interact with calf thymus DNA (ctDNA) through an intercalative mode. Interestingly enough, metal-driven molecular reorganizations serve to increase or decrease the biological activities of these compounds significantly.

Models MolecularCircular dichroismMacrocyclic CompoundsStereochemistryCell SurvivalDna interactionAntineoplastic AgentsNucleic Acid DenaturationBiochemistryCatalysisMetalchemistry.chemical_compoundColloid and Surface ChemistryCell Line TumorNeoplasmsAnimalsHumansBinding affinitiesCircular DichroismGeneral ChemistryDNAIntercalating AgentsDNA metabolismchemistryCell cultureMetalsvisual_artvisual_art.visual_art_mediumCattleSpectrophotometry UltravioletProtonsDNAJournal of the American Chemical Society
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Stability and disassembly properties of human naïve Hsp60 and bacterial GroEL chaperonins.

2015

Human Hsp60 chaperonin and its bacterial homolog GroEL, in association with the corresponding co-chaperonins Hsp10 and GroES, constitute important chaperone systems promoting the proper folding of several mitochondrial proteins. Hsp60 is also currently described as a ubiquitous molecule with multiple roles both in health conditions and in several diseases. Naïve Hsp60 bearing the mitochondrial import signal has been recently demonstrated to present different oligomeric organizations with respect to GroEL, suggesting new possible physiological functions. Here we present a combined investigation with circular dichroism and small-angle X-ray scattering of structure, self-organization, and sta…

guanidiniun chloride0301 basic medicineGuanidinium chlorideSmall AngleCircular dichroismBiophysicsmacromolecular substancesBiochemistryGroELChaperoninScatteringMitochondrial Proteins03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsX-Ray DiffractionScattering Small AngleHumansGuanidinebiologyProtein StabilityCircular DichroismOrganic ChemistryTemperatureGroESSAXSChaperonin 60Hsp60GroELSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)CDcited By 5enzymes and coenzymes (carbohydrates)Denaturation030104 developmental biologychemistryBiochemistryChaperone (protein)biological sciencesbiology.proteinCD; Denaturation; GroEL; Guanidinium chloride; Hsp60; SAXS; Bacterial Proteins; Chaperonin 60; Circular Dichroism; Humans; Mitochondrial Proteins; Protein Stability; Scattering Small Angle; Temperature; X-Ray DiffractionbacteriaHSP60Guanidinium chlorideBiophysical chemistry
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Titration of poly(dA-dT).poly(dA-dT) in solution at variable NaCl concentration

2004

CD and uv absorption data showed that high molecular weight poly(dA-dT) poly(dA-dT), at 298 K, undergoes an acid-induced transition from B-double helix to random coil in NaCl solutions of different concentrations, ranging from 0.005 to 0.600M. Similarly, titration of the polynucleotide with a strong base causes duplex-to-single strands transition. The base- and acid-induced transitions were both reversible by back-titration (with an acid or, respectively, with a base): the apparent pKa were the same in both directions. However, the number of protons per titratable site (adenine N1) required to reach half-denaturation was in great excess over the stoichiometric value; to a much larger extent…

poly(dA-dT) poly(dA-dT)uv spectroscopyacid denaturationbasic denaturationCD
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The Internal Dynamics and Early Adsorption Stages of Fibrinogen Investigated by Molecular Dynamics Simulations

2016

Fibrinogen, a plasma glycoprotein of vertebrates, plays an essential role in blood clotting by polymerizing into fibrin upon activation. It also contributes, upon adsorption on material surfaces, to determine their biocompatibility and has been implicated as a cause of thrombosis and inflammation at medical implants. Here we present the first fully atomistic simulations of the initial stages of the adsorption process of fibrinogen on mica and graphite surfaces. The simulations reveal a weak adsorption on mica that allows frequent desorption and reorientation events. This adsorption is driven by electrostatic interactions between the protein and the silicate surface as well as the counter io…

BiocompatibilitybiologyChemistryFibrinogenFibrinMolecular dynamicsAdsorptionDesorptionmedicineBiophysicsbiology.proteinDenaturation (biochemistry)Micamedicine.drug
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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
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Mutation screening for the prothrombin variant G20210A by melting point analysis with the Light Cycler system: atypical results, detection of the var…

2005

In the differential diagnosis of thrombophilic disorders genotyping of prothrombin and factor V are nowadays performed as a routine analysis. In the following we describe the unusual results of the mutation screening using melting point analysis for two patients and the consecutive detection of the mutation C20209T by sequencing the corresponding gene fragments. The molecular result is discussed with special respect to the medical history, ethnic background and clinical findings of both patients.

AdultMaleHot TemperatureDNA Mutational AnalysisClinical BiochemistryBiologyNucleic Acid DenaturationThrombophiliaPolymerase Chain Reactionlaw.inventionlawmedicineHumansPoint MutationThrombophiliaMedical historyGenotypingPolymerase chain reactionGeneticsPoint mutationBiochemistry (medical)Factor VSequence Analysis DNAHematologyGeneral Medicinemedicine.diseaseMutation (genetic algorithm)biology.proteinFemaleProthrombinDifferential diagnosisClinical and Laboratory Haematology
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4-4-20 anti-fluorescyl IgG Fab' recognition of membrane bound hapten: direct evidence for the role of protein and interfacial structure.

1995

The surface forces apparatus was used to identify the molecular forces that control the interactions of monoclonal 4-4-20 antifluorescyl IgG Fab' fragments with fluorescein-presenting supported planar bilayers. At long range, the electrostatic force between oriented Fab' and fluorescein monolayers was controlled by the composition of the protein exterior surrounding the antigen-combining site rather than by the overall protein charge. The measured positive electrostatic potential of the Fab' monolayer at pH > pI(Fab') was consistent with the structure of the exposed Fab' surface in which a ring of positive charge at the mouth of the antigen-combining site dominates the local electrostatic s…

Steric effectsProtein DenaturationChemistryStereochemistryProtein ConformationSurface PropertiesCell MembraneAntibodies MonoclonalSurface forces apparatusAdhesionFluoresceinsBiochemistryProtein–protein interactionAntigen-Antibody ReactionsImmunoglobulin Fab FragmentsMembraneProtein structureImmunoglobulin GMonolayerBiophysicsElectrochemistryFluoresceinHaptenHaptensBiochemistry
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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
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The interaction of native calf thymus DNA with FeIII-dipyrido[3,2-a:2’,3’-c]phenazine

2008

The mono and bis dipyrido[3,2-a:2',3'-c]phenazine (dppz) adducts of iron(III) chloride, i.e. [Fe(dppz)]Cl(3) and [Fe(dppz)(2)]Cl(3), have been synthesized and characterized. The interaction of the Fe(III)dppz hydrolyzed aquo complex with native calf thymus DNA has been monitored as a function of the metal complex-DNA molar ratio, by variable temperature UV absorption spectrophotometry, circular dichroism (CD) and fluorescence spectroscopy. The results obtained in solution at various ionic strength values give support for a tight intercalative binding of the Fe(III)dppz cation with DNA. In particular, the appearance of induced CD bands, caused by the addition of Fe(III)dppz, indicate the exi…

Circular dichroismDNA dppz Intercalation Iron SpectroscopyIntercalation (chemistry)PhenazinePhotochemistryNucleic Acid DenaturationBiochemistryFerric CompoundsFluorescenceAdductInorganic ChemistryMetalchemistry.chemical_compoundDNA AdductsMetal aquo complexChemistryCircular DichroismDNABinding constantCrystallographyIonic strengthSettore CHIM/03 - Chimica Generale E Inorganicavisual_artvisual_art.visual_art_mediumPhenazines
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Thermal induced conformational changes involved in the aggregation pathways of beta-lactoglobulin.

2004

Aggregation of proteins appears to be associated most often with conformational and structural changes that lead to exposure of some apolar residues. Depending on the native structure of the protein in exam, aggregation is a process that involves different mechanisms, whose time of occurrence and interplay can depend upon temperature. To single out information about the multistages of the aggregation pathway, here we investigate the thermally induced conformational and structural changes of the beta-lactoglobulin (BLG). The experimental approach consists in studying steady-state fluorescence spectra of intrinsic chromophores, two tryptophans, and Anylino-Naphthalene-Sulfonate dye (ANS) mole…

Models MolecularCircular dichroismProtein DenaturationChemistryProtein ConformationSpectrum AnalysisOrganic ChemistryKineticsIntermolecular forceBiophysicsTemperatureLactoglobulinsProtein aggregationChromophoreCrystallography X-RayBiochemistryFluorescenceHydrophobic effectCrystallographyKineticsProtein structureBiophysicsDimerizationBiophysical chemistry
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