Abstract
There is a great interest within the research community to understand the structure–function relationship for intrinsically disordered proteins (IDPs); however, the heterogeneous distribution of conformations that IDPs can adopt limits the applicability of conventional structural biology methods. Here, scattering techniques, such as small-angle X-ray scattering, can contribute. In this chapter, we will describe how to make a model-free determination of the radius of gyration by using two different approaches, the Guinier analysis and the pair distance distribution function. The ATSAS package (Franke et al., J Appl Crystallogr 50:1212–1225, 2017) has been used for the evaluation, and throughout the chapter, different examples will be given to illustrate the discussed phenomena, as well as the pros and cons of using the different approaches.
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Acknowledgments
We are grateful to Dr. Mark Tully at the European Synchrotron Radiation Facility (ESRF), Grenoble, France, and Dr. Samuel Lenton at the Division of Theoretical Chemistry, Lund University, Sweden, for valuable comments and proofreading of the text.
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Rieloff, E., Skepö, M. (2020). Determining Rg of IDPs from SAXS Data. In: Kragelund, B.B., Skriver, K. (eds) Intrinsically Disordered Proteins. Methods in Molecular Biology, vol 2141. Humana, New York, NY. https://doi.org/10.1007/978-1-0716-0524-0_13
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DOI: https://doi.org/10.1007/978-1-0716-0524-0_13
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