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| - Interconverting Conformations of Variants of theHuman Amyloidogenic Protein β2-MicroglobulinQuantitatively Characterized by Dynamic CapillaryElectrophoresis and Computer Simulation
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| - Capillary electrophoretic separation profiles of cleavedvariants of β2-microglobulin (β2m) reflect the conformational equilibria existing in solutions of these proteins.The characterization of these equilibria is of interest sinceβ2m is responsible for amyloid formation in dialysis-related amyloidosis and thus is able to attain alternativeconformations that lead to irreversible aggregation andprecipitation. In this study, we quantitate the increasedconformational instability of cleaved β2m by extracting rateconstants and activation energies by simulating the experimental data using a unified theory for dynamic chromatography and dynamic electrophoresis. The results arecorrelated with the outcome of independent experimentsbased on mass spectrometric measurement of H/D exchange. This study illustrates that dynamic capillaryelectrophoresis is suitable for the investigation of theinterconversion of protein conformations of amyloidogenicmolecules and is not only restricted to ideal modelcompounds.
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