Abstract
Fourier transform infrared (FTIR) spectroscopy is a useful tool for the structural characterization of insoluble protein assemblies, as it allows to obtain information on the protein secondary structures and on their intermolecular interactions. The protocols for FTIR spectroscopy and microspectroscopy measurements in transmission and attenuated total reflection modes will be presented and illustrated in the following examples: bacterial inclusion bodies, self-assembling peptides, thermal aggregates, and amyloid fibrils.
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Acknowledgment
In this work to illustrate the protocols for FTIR measurements of protein aggregates, we presented examples on proteins studied in collaborations with colleagues that we would like to acknowledge: Prof. Paolo Tortora, Prof. Angelo Vescovi, Dr. Diletta Ami, Dr. Maria E. Regonesi, and Dr. Fabrizio Gelain of the University of Milano-Bicocca, Prof. Martino Bolognesi and Dr. Stefano Ricagno of the University of Milan, and Prof. Vittorio Bellotti of the University of Pavia.
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Natalello, A., Doglia, S.M. (2015). Insoluble Protein Assemblies Characterized by Fourier Transform Infrared Spectroscopy. In: García-Fruitós, E. (eds) Insoluble Proteins. Methods in Molecular Biology, vol 1258. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-2205-5_20
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DOI: https://doi.org/10.1007/978-1-4939-2205-5_20
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