A thermodynamic study of the third PDZ domain of MAGUK neuronal protein PSD-95 reveals a complex three-state folding behavior

Javier Murciano-Calles, Jose C. Martinez, Marta Marin-Argany, Sandra Villegas, Eva S. Cobos

Research output: Contribution to journalArticleResearchpeer-review

8 Citations (Scopus)

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. © 2013 Elsevier B.V.
Original languageEnglish
Pages (from-to)1-7
JournalBiophysical Chemistry
Volume185
DOIs
Publication statusPublished - 1 Jan 2014

Keywords

  • Differential scanning calorimetry
  • Oligomeric intermediate
  • PDZ domain
  • Protein folding
  • Thermodynamics
  • Three-state model

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