A thermodynamic study of the third PDZ domain of MAGUK neuronal protein PSD-95 reveals a complex three-state folding behavior.
Biophys Chem
; 185: 1-7, 2014 Jan.
Article
em En
| MEDLINE
| ID: mdl-24295614
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.
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01-internacional
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MEDLINE
Assunto principal:
Termodinâmica
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Dobramento de Proteína
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Peptídeos e Proteínas de Sinalização Intracelular
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Domínios PDZ
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article