Determining Rg of IDPs from SAXS Data
(2020) In Methods in molecular biology (Clifton, N.J.) 2141. p.271-283- 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... (More)
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.
(Less)
- author
- Rieloff, Ellen LU and Skepö, Marie LU
- organization
- publishing date
- 2020
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- ATSAS, Flexible proteins, GNOM, Guinier, Intrinsically disordered proteins, Pair distance distribution function, PRIMUS, Radius of gyration, Scattering
- in
- Methods in molecular biology (Clifton, N.J.)
- volume
- 2141
- pages
- 13 pages
- publisher
- Springer
- external identifiers
-
- scopus:85088503301
- pmid:32696362
- ISSN
- 1940-6029
- DOI
- 10.1007/978-1-0716-0524-0_13
- language
- English
- LU publication?
- yes
- id
- 96d3bea3-cb02-45bb-87aa-2f8d0eeb6272
- date added to LUP
- 2020-08-05 12:41:09
- date last changed
- 2024-04-03 12:09:56
@article{96d3bea3-cb02-45bb-87aa-2f8d0eeb6272,
abstract = {{<p>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.</p>}},
author = {{Rieloff, Ellen and Skepö, Marie}},
issn = {{1940-6029}},
keywords = {{ATSAS; Flexible proteins; GNOM; Guinier; Intrinsically disordered proteins; Pair distance distribution function; PRIMUS; Radius of gyration; Scattering}},
language = {{eng}},
pages = {{271--283}},
publisher = {{Springer}},
series = {{Methods in molecular biology (Clifton, N.J.)}},
title = {{Determining R<sub>g</sub> of IDPs from SAXS Data}},
url = {{http://dx.doi.org/10.1007/978-1-0716-0524-0_13}},
doi = {{10.1007/978-1-0716-0524-0_13}},
volume = {{2141}},
year = {{2020}},
}