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• W2069220822 abstract "The relevance of the C-terminal α helix of the PDZ3 domain of PSD95 in its unfolding process has been explored by achieving the thermodynamic characterization of a construct where the sequence of the nine residues corresponding to such motif has been deleted. Calorimetric traces at neutral pH require the application of a three-state model displaying three different equilibrium processes in which the intermediate state self-associates upon heating, being stable and populated in a wide temperature range. Temperature scans followed by circular dichroism, Fourier transform infrared spectroscopy and dynamic light scattering support the presence of such oligomeric-partially folded species. This study reveals that the deletion of the α3-helix sequence results in a more complex description of the domain unfolding." @default.
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• W2069220822 date "2014-01-01" @default.
• W2069220822 modified "2023-10-17" @default.
• W2069220822 title "A thermodynamic study of the third PDZ domain of MAGUK neuronal protein PSD-95 reveals a complex three-state folding behavior" @default.
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• W2069220822 doi "https://doi.org/10.1016/j.bpc.2013.10.005" @default.
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• W2069220822 hasPublicationYear "2014" @default.
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