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Circular-Dichroism and Synchrotron-Radiation Circular-Dichroism Spectroscopy as Tools to Monitor Protein Structure in a Lipid Environment

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Lipid-Protein Interactions

Part of the book series: Methods in Molecular Biology ((MIMB,volume 974))

Abstract

Circular-dichroism (CD) spectroscopy is a powerful tool for the secondary-structure analysis of proteins. The structural information obtained by CD does not have atomic-level resolution (unlike X-ray crystallography and NMR spectroscopy), but it has the great advantage of being applicable to both nonnative and native proteins in a wide range of solution conditions containing lipids and detergents. The development of synchrotron-radiation CD (SRCD) instruments has greatly expanded the utility of this method by extending the spectra to the vacuum-ultraviolet region below 190 nm and producing information that is unobtainable by conventional CD instruments. Combining SRCD data with bioinformatics provides new insight into the conformational changes of proteins in a membrane environment.

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Authors and Affiliations

  1. Hiroshima Synchrotron Radiation Center, Hiroshima University, Higashi-Hiroshima, Japan

    Koichi Matsuo

  2. Institute for Sustainable Sciences and Development, Hiroshima University, Higashi-Hiroshima, Japan

    Kunihiko Gekko

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  1. Koichi Matsuo
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  2. Kunihiko Gekko
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Correspondence to Kunihiko Gekko .

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  1. Institut für Biologie, Abteilung Biophysik, Universität Kassel, Heinrich-Plett-Straße 40, Kassel, 34132, Germany

    Jörg H. Kleinschmidt

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Matsuo, K., Gekko, K. (2013). Circular-Dichroism and Synchrotron-Radiation Circular-Dichroism Spectroscopy as Tools to Monitor Protein Structure in a Lipid Environment. In: Kleinschmidt, J. (eds) Lipid-Protein Interactions. Methods in Molecular Biology, vol 974. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-275-9_8

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  • DOI: https://doi.org/10.1007/978-1-62703-275-9_8

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