Hydrophobins, hfb2, are secreted fungal proteins in the form of a small lipopeptide. They are strongly surface active and self-assemble in solution and at interfaces. They have great potential as stabilisers in food related foam and emulsion formulations, where they will be invariably used in conjunction with other proteins, such as beta-casein. Their solution self-assembly with beta-casein is the focus of this proposal. Initial SANS and light scattering, LS, studies on beta-casein and beta-casein / hydrophobin mixtures suggest that the size range is larger than that accessible with conventional SANS and that LS does not provide the required selectivity. We request bean time on offSPEC to probe a larger size range using SEESANS.