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

I. Assignments and Model Compounds

  • Chapter
Physicochemical Methods in the Study of Biomembranes

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

Abstract

During the last five years, the use of infrared spectroscopy (IR)* to determine the structure of biological materials has dramatically expanded. However, IR’s biggest advantage and highest potential over older techniques is in analyzing the components of biological membranes. IR is technically simple, requires little material (less than 0.1 μg) when attenuated total reflection spectroscopy (ATR) is used. Spectra are recorded in a matter of minutes; the environment of the studied molecules can be modified so that their conformation can be studied as a function of temperature, pressure, and pH, as well as in the presence of specific ligands. Because of IR’s long wavelength, light scattering problems are virtually nonexistent, and highly aggregated materials or large membrane fragments can be studied. Secondary structure evaluation is in most cases affected by neither amino acid side chains nor by the presence of disulfide bridges. In addition to the conformational parameters which can be deduced from the shape of the infrared spectra, the orientation of several molecular axes can be computed with polarized infrared spectroscopy. This allows more precise analysis of the general architecture of the membrane molecules within the biological membranes. The unique advantage of IR is that it allows simultaneous study of the structure of lipids and proteins in intact biological membranes without introduction of foreign probes.

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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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Editors and Affiliations

  1. University of Antwerp, Antwerp, Belgium

    Herwig J. Hilderson

  2. University of Sydney, Sydney, Australia

    Gregory B. Ralston

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© 1994 Springer Science+Business Media New York

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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_8

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  • DOI: https://doi.org/10.1007/978-1-4615-1863-1_8

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5757-5

  • Online ISBN: 978-1-4615-1863-1

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