The statistical conformation of a highly flexible protein: small-angle X-ray scattering of S. aureus protein A.
Journal Article (Journal Article)
Staphylococcal protein A (SpA) is a multidomain protein consisting of five globular IgG binding domains separated by a conserved six- to nine-residue flexible linker. We collected SAXS data on the N-terminal protein-binding half of SpA (SpA-N) and constructs consisting of one to five domain modules in order to determine statistical conformation of this important S. aureus virulence factor. We fit the SAXS data to a scattering function based on a new polymer physics model, which provides an analytical description of the SpA-N statistical conformation. We describe a protocol for systematically determining the appropriate level of modeling to fit a SAXS data set based on goodness of fit and whether the addition of parameters improves it. In the case of SpA-N, the analytical polymer physics description provides a depiction of the statistical conformation of a flexible protein that, while lacking atomistic detail, properly reflects the information content of the data.
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Duke Authors
Cited Authors
- Capp, JA; Hagarman, A; Richardson, DC; Oas, TG
Published Date
- August 5, 2014
Published In
Volume / Issue
- 22 / 8
Start / End Page
- 1184 - 1195
PubMed ID
- 25087509
Pubmed Central ID
- PMC4172662
Electronic International Standard Serial Number (EISSN)
- 1878-4186
Digital Object Identifier (DOI)
- 10.1016/j.str.2014.06.011
Language
- eng
Conference Location
- United States