The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

Photo Marie Skepö

Marie Skepö

Professor

Photo Marie Skepö

Determining Rg of IDPs from SAXS Data

Author

  • Ellen Rieloff
  • Marie Skepö

Summary, in English

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.

Department/s

  • Computational Chemistry
  • eSSENCE: The e-Science Collaboration

Publishing year

2020

Language

English

Pages

271-283

Publication/Series

Methods in molecular biology (Clifton, N.J.)

Volume

2141

Document type

Journal article

Publisher

Springer

Topic

  • Structural Biology

Keywords

  • ATSAS
  • Flexible proteins
  • GNOM
  • Guinier
  • Intrinsically disordered proteins
  • Pair distance distribution function
  • PRIMUS
  • Radius of gyration
  • Scattering

Status

Published

ISBN/ISSN/Other

  • ISSN: 1940-6029