Search results for "Thermal irreversibility"

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Irreversible gelation of thermally unfolded proteins:structural and mechanical properties of lysozyme aggregates

2010

The formation of protein aggregates is important in many fields of life science and technology. The morphological and mechanical properties of protein solutions depend upon the molecular conformation and thermodynamic and environmental conditions. Non-native or unfolded proteins may be kinetically trapped into irreversible aggregates and undergo precipitation or gelation. Here, we study the thermal aggregation of lysozyme in neutral solutions. We characterise the irreversible unfolding of lysozyme by differential scanning calorimetry. The structural properties of aggregates and their mechanisms of formation with the eventual gelation are studied at high temperature by spectroscopic, rheolog…

Models MolecularProtein FoldingCircular dichroismGelationProtein ConformationDiffusionBiophysicsProtein aggregationUnfoldingchemistry.chemical_compoundDifferential scanning calorimetryProtein structureAnimalsQuantitative Biology::BiomoleculesChemistryPrecipitation (chemistry)Circular DichroismTemperaturePercolationGeneral MedicineBlood Coagulation FactorsSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)Thermal irreversibilityCrystallographyChemical physicsThermodynamicsMuramidaseProtein foldingLysozymeProtein aggregation
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