Infrared spectroscopy has been proved to be a powerful tool to study protein conformation and dynamics and, therefore, to characterize the structural properties of intrinsically disordered proteins (IDPs) and their induced folding in different environmental conditions. In this chapter, we present a general survey of the standard experimental methods to obtain the infrared absorption spectrum of a protein. The procedures required to identify the protein absorption components in the amide I region (1700 - 1600 cm - 1 ) and to assign them to the secondary structures are discussed, together with the data analysis that enable to evaluate the secondary structure content. Interestingly, this spectroscopy allows to examine proteins in different environmental conditions, both in solution and in solid form as protein films. We illustrate the potential of infrared spectroscopy on selected studies of IDP - induced folding by different effectors, such as DNA, partner proteins, and osmolytes. IDPs undergoing amyloid aggregation, as a - synuclein and a prion peptide, are also reported. © 2010 John Wiley and Sons, Inc.

Natalello, A., Doglia, S. (2010). Intrinsically Disordered Proteins and Induced Folding Studied by Fourier Transform Infrared Spectroscopy. In Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (pp. 225-252). John Wiley and Sons [10.1002/9780470602614.ch8].

Intrinsically Disordered Proteins and Induced Folding Studied by Fourier Transform Infrared Spectroscopy

NATALELLO, ANTONINO
;
DOGLIA, SILVIA MARIA
Ultimo
2010

Abstract

Infrared spectroscopy has been proved to be a powerful tool to study protein conformation and dynamics and, therefore, to characterize the structural properties of intrinsically disordered proteins (IDPs) and their induced folding in different environmental conditions. In this chapter, we present a general survey of the standard experimental methods to obtain the infrared absorption spectrum of a protein. The procedures required to identify the protein absorption components in the amide I region (1700 - 1600 cm - 1 ) and to assign them to the secondary structures are discussed, together with the data analysis that enable to evaluate the secondary structure content. Interestingly, this spectroscopy allows to examine proteins in different environmental conditions, both in solution and in solid form as protein films. We illustrate the potential of infrared spectroscopy on selected studies of IDP - induced folding by different effectors, such as DNA, partner proteins, and osmolytes. IDPs undergoing amyloid aggregation, as a - synuclein and a prion peptide, are also reported. © 2010 John Wiley and Sons, Inc.
Capitolo o saggio
IDPs and induced folding by FT-IR spectroscopy; Intrinsically disordered proteins and induced folding - by Fourier transform infrared spectroscopy; Late embryogenesis abundant (LEA) proteins - IDPs, role in desiccation tolerance in plants and seeds; Biochemistry, Genetics and Molecular Biology (all)
English
Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation
9780470343418
Natalello, A., Doglia, S. (2010). Intrinsically Disordered Proteins and Induced Folding Studied by Fourier Transform Infrared Spectroscopy. In Instrumental Analysis of Intrinsically Disordered Proteins: Assessing Structure and Conformation (pp. 225-252). John Wiley and Sons [10.1002/9780470602614.ch8].
Natalello, A; Doglia, S
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/10281/138712
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