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Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy

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Abstract

Circular dichroism (CD) spectroscopy is a fast, powerful, well-established, and widely used analytical technique in the biophysical and structural biology community to study protein secondary structure and to track changes in protein conformation in different environments. The use of the intense light of a synchrotron beam as the light source for collecting CD measurements has emerged as an enhanced method, known as synchrotron radiation circular dichroism (SRCD) spectroscopy, that has several advantages over the conventional CD method, including a significant spectral range extension for data collection, deeper access to the lower limit (cut-off) of conventional CD spectroscopy, an improved signal-to-noise ratio to increase accuracy in the measurements, and the possibility to collect measurements in highly absorbing solutions. In this review, we discuss different applications of the SRCD technique by researchers from Latin America. In this context, we specifically look at the use of this method for examining the secondary structure and conformational behavior of proteins belonging to the four main classes of the hierarchical protein domain classification CATH (Class, Architecture, Topology, Homology) database, focusing on the advantages and improvements associated with SRCD spectroscopy in terms of characterizing proteins composed of different structural elements.

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Acknowledgements

JLSL and PSK are grateful for beamtime access at the AU-CD beamline at the ASTRID2 (Aarhus, Denmark) and at the UV-CD12 at t he ANKA (Karlsruhe, Germany) synchrotrons. All authors thank Prof. BA Wallace for supporting the implementation of SRCD in Brazil and for helpful discussions.

Funding

We thank following institutions for providing financial support in the form of grants: Sao Paulo Research Foundation (FAPESP) grants 15/50347-2 (to APUA), National Council for Scientific and Technological Development (CNPq) grants 150417/2016-0 (to PSK), 407337/2013-0 (to APUA) and 303513/2016-0 (to JLSL)

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Authors and Affiliations

  1. Instituto de Física de São Carlos, Universidade de São Paulo, São Paulo, SP, Brazil

    Patricia S. Kumagai & Ana P. U. Araujo

  2. Departamento Física Aplicada, Instituto de Física,, Universidade de São Paulo, Rua do Matão 1371, Cidade Universitária, São Paulo, SP, 05508-090, Brazil

    Jose L. S. Lopes

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  1. Patricia S. Kumagai
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  2. Ana P. U. Araujo
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  3. Jose L. S. Lopes
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Correspondence to Jose L. S. Lopes.

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This article does not contain any studies with human participants or animals performed by any of the authors.

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This article is part of a Special Issue on ‘Latin America’ edited by Pietro Ciancaglini and Rosangela Itri.

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Kumagai, P.S., Araujo, A.P.U. & Lopes, J.L.S. Going deep into protein secondary structure with synchrotron radiation circular dichroism spectroscopy. Biophys Rev 9, 517–527 (2017). https://doi.org/10.1007/s12551-017-0314-2

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