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Experimental Determination of Membrane Protein Secondary Structure Using Vibrational and CD Spectroscopies

  • Chapter
Membrane Protein Structure

Part of the book series: Methods in Physiology Series ((METHPHYS))

Abstract

Experimentalists interested in obtaining spectroscopic measurements of membrane protein secondary structure must keep in mind one general critical issue: the measurements must be reliable and specific enough to help distinguish between competing models of structure or function. An example of how this issue plays itself out can be seen in a series of papers beginning with that of Jap et al. (1983), in which it was proposed that some of the images in the in-plane electron diffraction map of bacteriorhodopsin may be due to transmembrane β-sheets instead of helices. This proposal was supported by circular dichroism (CD) and infrared (IR) measurements of secondary structures. The calculated helix content was only about 50%, and β-sheet content was about 20%. The investigators carefully corrected for differential light scattering in their CD measurements, but (according to subsequent studies) did not correct for absorption flattening effects. IR spectra were clearly not consistent with the hypothesis that the protein was 80% helix. The amide I maximum was at about 1,686 cm−1, while an 80% helical protein should have an amide I maximum at about 1,652 cm−1. Other CD results by Wallace and Mao (1984) that corrected for the absorption flattening effects did not support the β-sheet hypothesis. Their calculated helix content was about 80%. However, this calculation included a normalization of the results to correct for what was assumed to be an inaccurate determination of protein concentration. The data upon which it was based was actually similar to those obtained by Jap et al. (1983). Glaeser and Jap (1985) subsequently made a convincing argument that the normalization procedure was not valid. Nevertheless, in the face of recent evidence, Glaeser et al. (1991) subsequently acknowledged that all of the transmembrane segments are clearly helical and that their β-sheet hypothesis was wrong.

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  1. Robert W. Williams
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  1. College of Medicine, Department of Physiology and Biophysics, University of California, Irvine, Irvine, California, USA

    Stephen H. White Ph.D. (Professor of Physiology and Biophysics) (Professor of Physiology and Biophysics)

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Williams, R.W. (1994). Experimental Determination of Membrane Protein Secondary Structure Using Vibrational and CD Spectroscopies. In: White, S.H. (eds) Membrane Protein Structure. Methods in Physiology Series. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-7515-6_8

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  • DOI: https://doi.org/10.1007/978-1-4614-7515-6_8

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