Search results for " Protein Stability"

showing 6 items of 6 documents

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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The increase in maternal expression of axin1 and axin2 contribute to the zebrafish mutant ichabod ventralized phenotype.

2014

β-Catenin is a central effector of the Wnt pathway and one of the players in Ca(+)-dependent cell-cell adhesion. While many wnts are present and expressed in vertebrates, only one β-catenin exists in the majority of the organisms. One intriguing exception is zebrafish that carries two genes for β-catenin. The maternal recessive mutation ichabod presents very low levels of β-catenin2 that in turn affects dorsal axis formation, suggesting that β-catenin1 is incapable to compensate for β-catenin2 loss and raising the question of whether these two β-catenins may have differential roles during early axis specification. Here we identify a specific antibody that can discriminate selectively for β-…

axin1axin2zebrafish mutant ichabodMessengerEmbryonic DevelopmentBiochemistryBETA-CATENINAxin2-RGS DOMAINAxin ProteinAntibody SpecificitySettore BIO/10 - BiochimicaAnimalsAxin2-RGS DOMAIN; AXIS FORMATION; BETA-CATENIN; Wnt signaling; ZEBRAFISH; Animals; Antibody Specificity; Axin Protein; Blastula; Cell Nucleus; Embryonic Development; Female; Gene Expression Regulation Developmental; Genes Dominant; Immunohistochemistry; Lithium Chloride; Mutation; Phenotype; Protein Stability; Protein Transport; RNA Messenger; Signal Transduction; Up-Regulation; Zebrafish; Zebrafish Proteins; beta Catenin; Biochemistry; Cell Biology; Molecular BiologyDevelopmentalDominantRNA MessengerMolecular BiologyZebrafishbeta CateninGenes DominantAXIS FORMATIONCell NucleusProtein StabilityGene Expression Regulation DevelopmentalCell BiologyBlastulaZebrafish ProteinsWnt signalingImmunohistochemistryUp-RegulationProtein TransportPhenotypeGene Expression RegulationGenesMutationRNAFemaleLithium ChlorideSignal Transduction
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Thioflavin T templates amyloid β(1–40) conformation and aggregation pathway

2015

Aβ(1-40) peptide supramolecular assembly and fibril formation processes are widely recognized to have direct implications in the progression of Alzheimer's disease. The molecular basis of this biological process is still unknown and there is a strong need of developing effective strategies to control the occurring events. To this purpose the exploitation of small molecules interacting with Aβ aggregation represents one of the possible routes. Moreover, the use specific labeling has represented so far one of the most common and effective methods to investigate such a process. This possibility in turn rests on the reliability of the probe/labels involved. Here we present evidences of the effe…

Protein StructureSecondaryAβ(1–40) peptideAmyloidProtein ConformationMolecular Sequence DataBiophysicsSupramolecular chemistryMolecular Dynamics SimulationProtein aggregationProtein Aggregation PathologicalBiochemistryProtein Structure SecondarySupramolecular assemblyProtein Aggregateschemistry.chemical_compoundProtein structureAlzheimer DiseasePathologicalSecondary structureAβ(1-40) peptideHumansBenzothiazolesAmino Acid SequenceFluorescent DyesAmyloid beta-PeptidesProtein StabilityOrganic ChemistryAlzheimer's diseaseProtein AggregationSmall moleculePeptide FragmentsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Peptide ConformationAlzheimer's disease; Aβ(1–40) peptide; Protein aggregation; Protein conformation; Secondary structure; Thioflavin T; Alzheimer Disease; Amino Acid Sequence; Amyloid beta-Peptides; Fluorescence Recovery After Photobleaching; Fluorescent Dyes; Humans; Molecular Dynamics Simulation; Molecular Sequence Data; Peptide Fragments; Protein Aggregates; Protein Aggregation Pathological; Protein Conformation; Protein Multimerization; Protein Stability; Protein Structure Secondary; ThiazolesThiazolesBiophysicBiochemistrychemistryThioflavin TBiophysicsThioflavinProtein MultimerizationFluorescence Recovery After PhotobleachingBiophysical Chemistry
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HSA Oxidation ImprovesThermal Stability and InhibitsAmyloid Fibril Formation

2014

amyloid aminoacid oxidation protein stability
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Halloysite nanotubes for efficient loading, stabilization and controlled release of insulin

2018

Hypothesis: Oral insulin administration is not actually effective due to insulin rapid degradation, inactivation and digestion by proteolytic enzymes which results in low bioavailability. Moreover insulin is poorly permeable and lack of lipophilicity. These limits can be overcome by the loading of protein in some nanostructured carrier such as halloysite nanotubes (HNTs). Experiments: Herein we propose an easy strategy to obtain HNT hybrid materials for the delivery of insulin. We report a detailed description on the thermal behavior and stability of insulin loaded and released from the HNTs hybrid by the combination of several techniques. Findings: Release experiments of insulin from the H…

Dichroismmedicine.medical_treatmentHalloysite nanotube02 engineering and technology01 natural sciencesBiochemistryNanocompositesChitosanchemistry.chemical_compoundColloid and Surface ChemistryDrug StabilityProtein stabilityHalloysite nanotube (HNTs)InsulinTransdermalSettore CHIM/02 - Chimica FisicaDrug CarriersNanotubesProteolytic enzymes021001 nanoscience & nanotechnologyControlled releaseSurfaces Coatings and FilmsElectronic Optical and Magnetic MaterialsEnzyme inhibitionAluminum SilicatesBionanocomposite film0210 nano-technologyHybrid materialBionanocomposite hybridSurface PropertiesDrug Compoundingengineering.materialCircular dichroism data010402 general chemistrySustained release InsulinAdministration CutaneousHalloysiteBiomaterialsKaolinitemedicineParticle SizeHybrid materialChitosanInsulinBiomedical applicationMedical applicationYarn Bio-nanocompositeMembranes Artificial0104 chemical sciencesNanotubeDrug LiberationHalloysite nanotubes Insulin Protein stability Sustained release Bionanocomposite hybridchemistryChemical engineeringDelayed-Action PreparationsengineeringClayNanocarriersSustained release
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Atomic mean square displacements in proteins by Molecular Dynamics: a case for analysis of variance

2004

Information on protein internal motions is usually obtained through the analysis of atomic mean-square displacements, which are a measure of variability of the atomic positions distribution functions. We report a statistical approach to analyze molecular dynamics data on these displacements that is based on probability distribution functions. Using a technique inspired by the analysis of variance, we compute unbiased, reliable mean-square displacements of the atoms and analyze them statistically. We applied this procedure to characterize protein thermostability by comparing the results for a thermophilic enzyme and a mesophilic homolog. In agreement with previous experimental observations, …

Proteins Protein Stabilitythermophilic proteins
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