Search results for "Native state"

showing 2 items of 12 documents

Unlocked Concanavalin A Forms Amyloid-like Fibrils from Coagulation of Long-lived "Crinkled'' Intermediates

2013

Understanding the early events during amyloid aggregation processes is crucial to single out the involved molecular mechanisms and for designing ad hoc strategies to prevent and reverse amyloidogenic disorders. Here, we show that, in conditions in which the protein is positively charged and its conformational flexibility is enhanced, Concanavalin A leads to fibril formation via a non-conventional aggregation pathway. Using a combination of light scattering, circular dichroism, small angle X-ray scattering, intrinsic (Tryptophan) and extrinsic (ANS) fluorescence and confocal and 2-photon fluorescence microscopy we characterize the aggregation process as a function of the temperature. We high…

Macromolecular AssembliesProteomicsCircular dichroismProtein StructureAmyloidProtein FoldingScienceMedical BiotechnologyBiophysics02 engineering and technologyFibrilBiochemistryProtein Chemistry03 medical and health sciencesProtein structureMedicinsk bioteknologiFluorescence microscopeNative stateConcanavalin ACoagulation (water treatment)Protein InteractionsBiology030304 developmental biology0303 health sciencesprotein aggregation amyloid concanavalin A intermediates spectroscopy advanced fluorescence microscopyMultidisciplinaryChemical PhysicsChemistryPhysicsCircular DichroismQRProteins021001 nanoscience & nanotechnologyProtein Structure TertiaryLuminescent ProteinsBiochemistryBiophysicsMedicineProtein folding0210 nano-technologyHydrophobic and Hydrophilic InteractionsFunction (biology)Research Article
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On the polymer physics origins of protein folding thermodynamics

2016

A remarkable feature of the spontaneous folding of many small proteins is the striking similarity in the thermodynamics of the folding process. This process is characterized by simple two-state thermodynamics with large and compensating changes in entropy and enthalpy and a funnel-like free energy landscape with a free-energy barrier that varies linearly with temperature. One might attribute the commonality of this two-state folding behavior to features particular to these proteins (e.g., chain length, hydrophobic/hydrophilic balance, attributes of the native state) or one might suspect that this similarity in behavior has a more general polymer-physics origin. Here we show that this behavi…

Models Molecular0301 basic medicineProtein FoldingQuantitative Biology::BiomoleculesPolymersProtein ConformationChemistryEnthalpyTemperatureGeneral Physics and AstronomyEnergy landscapeThermodynamicsContact order03 medical and health sciences030104 developmental biologyNative statePolymer physicsProtein foldingDownhill foldingFolding funnelPhysical and Theoretical ChemistryThe Journal of Chemical Physics
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