Puroindoline-a, a lipid binding protein from common wheat, spontaneously forms prolate protein micelles in solution
Clifton, L. A., Sanders, M. R., Castelletto, V., Rogers, S. E., Heenan, R. K., Neylon, C., Frazier, R. and Green, R. J. (2011) Puroindoline-a, a lipid binding protein from common wheat, spontaneously forms prolate protein micelles in solution. Physical Chemistry Chemical Physics, 13 (19). pp. 8881-8888. ISSN 1463-9076
Full text not archived in this repository.
To link to this item DOI: 10.1039/c0cp02247k
The self-assembly in solution of puroindoline-a (Pin-a), an amphiphilic lipid binding protein from common wheat, was investigated by small angle neutron scattering, dynamic light scattering and size exclusion chromatography. Pin-a was found to form monodisperse prolate ellipsoidal micelles with a major axial radius of 112 +/- 4.5 A ˚ and minor axial radius of 40.4 +/- 0.18 A ˚ . These protein micelles were formed by the spontaneous self-assembly of 38 Pin-a molecules in solution and were stable over a wide pH range (3.5–11) and at elevated temperatures (20–65 degC). Pin-a micelles could be disrupted upon addition of the non-ionic surfactant dodecyl-b-maltoside, suggesting that the protein self-assembly is driven by hydrophobic forces, consisting of intermolecular interactions between Trp residues located within a well-defined Trp-rich domain of Pin-a.