Determining Rg of IDPs from SAXS Data

Ellen Rieloff, Marie Skepö

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskriftPeer review

Sammanfattning

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.

Originalspråkengelska
Sidor (från-till)271-283
Antal sidor13
TidskriftMethods in molecular biology (Clifton, N.J.)
Volym2141
DOI
StatusPublished - 2020

Ämnesklassifikation (UKÄ)

  • Strukturbiologi

Fingeravtryck

Utforska forskningsämnen för ”Determining Rg of IDPs from SAXS Data”. Tillsammans bildar de ett unikt fingeravtryck.

Citera det här