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Determination of Soluble and Membrane Protein Structure by Fourier Transform Infrared Spectroscopy

II. Experimental Aspects, Side Chain Structure, and H/D Exchange

  • Chapter
Physicochemical Methods in the Study of Biomembranes

Part of the book series: Subcellular Biochemistry ((SCBI,volume 23))

Abstract

Increasingly, infrared spectra discussed in the literature are modified by mathematical treatments such as smoothing or deconvolution which respectively destroy or enhance defined original features of the raw spectra. In some instances, features that do not belong to the protein spectrum are modified in such a way that they now seem to belong, leading to flawed interpretation of the results. Here we summarize the main causes of interference in protein spectra in relation to the experimental set up used for the recording of the spectra.

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Authors and Affiliations

  1. Laboratoire de Chimie Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, B-1050, Brussels, Belgium

    Erik Goormaghtigh, Véronique Cabiaux & Jean-Marie Ruysschaert

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  1. Erik Goormaghtigh
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  2. Véronique Cabiaux
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  3. Jean-Marie Ruysschaert
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  1. University of Antwerp, Antwerp, Belgium

    Herwig J. Hilderson

  2. University of Sydney, Sydney, Australia

    Gregory B. Ralston

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Goormaghtigh, E., Cabiaux, V., Ruysschaert, JM. (1994). Determination of Soluble and Membrane Protein Structure by Fourier Transform Infrared Spectroscopy. In: Hilderson, H.J., Ralston, G.B. (eds) Physicochemical Methods in the Study of Biomembranes. Subcellular Biochemistry, vol 23. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1863-1_9

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  • DOI: https://doi.org/10.1007/978-1-4615-1863-1_9

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