Evidence for self-association of a miniaturized version of agrin from hydrodynamic and small-angle X-ray scattering measurements

Patel, Trushar R., Besong, Tabot M. D., Patel, Nehal, Meier, Markus, Harding, Stephen E., Winzor, Donald J. and Stetefeld, Jorg (2011) Evidence for self-association of a miniaturized version of agrin from hydrodynamic and small-angle X-ray scattering measurements. Journal of Physical Chemistry B, 115 38: 11286-11293. doi:10.1021/jp206377b


Author Patel, Trushar R.
Besong, Tabot M. D.
Patel, Nehal
Meier, Markus
Harding, Stephen E.
Winzor, Donald J.
Stetefeld, Jorg
Title Evidence for self-association of a miniaturized version of agrin from hydrodynamic and small-angle X-ray scattering measurements
Journal name Journal of Physical Chemistry B   Check publisher's open access policy
ISSN 1520-6106
Publication date 2011-09
Sub-type Article (original research)
DOI 10.1021/jp206377b
Volume 115
Issue 38
Start page 11286
End page 11293
Total pages 8
Place of publication Washington, DC United States
Publisher American Chemical Society
Collection year 2012
Language eng
Formatted abstract
Hydrodynamic studies of miniagrin indicate a molar mass that is 20% larger than the value calculated from the sequence of this genetically engineered protein. Consistent with this finding is the negative sign and also the magnitude of the second virial coefficient obtained from small-angle X-ray scattering measurements. The inference that miniagrin reversibly self-associates is confirmed by a sedimentation equilibrium study that yields an equilibrium constant of 0.24 L/g for a putative monomer-dimer interaction. Finally, Guinier analysis of the small-angle X-ray scattering (SAXS) results yields concentration-dependent values for the radius of gyration that may be described by the monomer-dimer model and respective Rg values of 40 and 105 Å for the monomeric and dimeric miniagrin species. Although intermolecular protein interactions are endemic in the events leading to acetylcholine receptor aggregation by agrin, the matrix proteoglycan of which miniagrin is a miniaturized model, this investigation raises the possibility that agrin may itself self-associate. © 2011 American Chemical Society.
Keyword 2nd Virial-Coefficients
Flavus Urate Oxidase
Sedimentation Equilibrium
Protein Interactions
Muscular-Dystrophy
Alpha-Dystroglycan
Ionic-Strength
Messenger-Rna
Binding Site
Laminin
Q-Index Code C1
Q-Index Status Confirmed Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2012 Collection
ERA 2012 Admin Only
School of Chemistry and Molecular Biosciences
 
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