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Evidence for Self-Association of a Miniaturized Version of Agrin from Hydrodynamic and Small-Angle X-ray Scattering Measurements

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Department of Chemistry, University of Manitoba, Winnipeg, Manitoba, R3T 2N2, Canada
National Centre for Macromolecular Hydrodynamics, University of Nottingham, Sutton Bonington, LE12 5RD, United Kingdom
§ Department of Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, R3E 0J9, Canada
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane, Queensland 4072, Australia
E-mail [email protected]. Tel.: + 1 204 4747172. Fax: +1 204 4747608.
Cite this: J. Phys. Chem. B 2011, 115, 38, 11286–11293
Publication Date (Web):August 22, 2011
https://doi.org/10.1021/jp206377b
Copyright © 2011 American Chemical Society

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    Abstract

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    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.

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    Cited By

    This article is cited by 5 publications.

    1. Trushar R. Patel, Tabot M. D. Besong, Markus Meier, Kevin McEleney, Stephen E. Harding, Donald J. Winzor, Jörg Stetefeld. Interaction studies of a protein and carbohydrate system using an integrated approach: a case study of the miniagrin–heparin system. European Biophysics Journal 2018, 47 (7) , 751-759. https://doi.org/10.1007/s00249-018-1291-5
    2. Damien Hall, Stephen E. Harding. Foreword to ‘Quantitative and analytical relations in biochemistry’—a special issue in honour of Donald J. Winzor’s 80th birthday. Biophysical Reviews 2016, 8 (4) , 269-277. https://doi.org/10.1007/s12551-016-0227-5
    3. Stephen Harding, Richard Gillis, Fahad Almutairi, Tayyibe Erten, M. Kök, Gary Adams. Recent Advances in the Analysis of Macromolecular Interactions Using the Matrix-Free Method of Sedimentation in the Analytical Ultracentrifuge. Biology 2015, 4 (1) , 237-250. https://doi.org/10.3390/biology4010237
    4. Trushar R. Patel, Claudia Bernards, Markus Meier, Kevin McEleney, Donald J. Winzor, Manuel Koch, Jörg Stetefeld. Structural elucidation of full-length nidogen and the laminin–nidogen complex in solution. Matrix Biology 2014, 33 , 60-67. https://doi.org/10.1016/j.matbio.2013.07.009
    5. Trushar R. Patel, Donald J. Winzor. The macromolecular state of A‐kinase anchoring protein. Journal of Molecular Recognition 2012, 25 (1) , 11-14. https://doi.org/10.1002/jmr.1164

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