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Fourier transform infrared spectroscopy of intrinsically disordered proteins: measurement procedures and data

Antonino Natalello1, Diletta Ami, Silvia Maria Doglia

  • 1Department of Biotechnology and Biosciences, University of Milano-Bicocca, Milan, Italy. antonino.natalello@unimib.it

Methods in Molecular Biology (Clifton, N.J.)
|July 5, 2012
PubMed

A peculiar property of intrinsically disordered proteins (IDPs), or of intrinsically disordered domains, is the absence of a well-defined three dimensional structure under native conditions. Moreover, IDPs usually acquire a specific structure in the presence of different interactors. In this framework, Fourier transform infrared (FTIR) spectroscopy is a powerful tool to assess the disordered character of a protein and to study its induced folding. In this chapter, we will show the detailed experimental procedures to measure the FTIR spectra of protein samples and the spectral analyses required to obtain information on the protein secondary structures and aggregation.

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