Amphiphilic protein surfactant interactions are becoming increasingly important in all aspects of soft condensed matter for drug delivery, flavour enhancement, foam stability and emulsification and yet a full understanding the nature and mechanism of protein-surfactant interactions at the hydrophobic air water, oil water interfaces and in solution remains elusive. We have recently observed synergistic and competitive adsorption of the class 2 fungal protein Hydrophobin HFBII with Tween like ethoxylated surfactants at the air water interface and hydrophobic liquid solid interfaces. In order to fully understand the mechanism of adsorption we now need to study how these surfactants aggregate in bulk solution, particularly their structure. This is part of the basis of an industrial collaborative research agreement between Unilever R&D, ISIS and University of Oxford (PS-2011-1238).