Determining Rg of IDPs from SAXS Data

Ellen Rieloff; Marie Skepö

doi:10.1007/978-1-0716-0524-0_13

Determining R_g of IDPs from SAXS Data

Methods Mol Biol. 2020:2141:271-283. doi: 10.1007/978-1-0716-0524-0_13.

Authors

Ellen Rieloff¹, Marie Skepö²

Affiliations

¹ Division of Theoretical Chemistry, Department of Chemistry, Lund University, Lund, Sweden.
² Division of Theoretical Chemistry, Department of Chemistry, Lund University, Lund, Sweden. marie.skepo@teokem.lu.se.

PMID: 32696362
DOI: 10.1007/978-1-0716-0524-0_13

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.

Keywords: ATSAS; Flexible proteins; GNOM; Guinier; Intrinsically disordered proteins; PRIMUS; Pair distance distribution function; Radius of gyration; Scattering.

MeSH terms

Algorithms
Histatins / chemistry
Intrinsically Disordered Proteins / chemistry*
Scattering, Small Angle*
X-Ray Diffraction*

Substances

Histatins
Intrinsically Disordered Proteins