The phase behavior and structural properties of "protein limit" mixtures of small (radius 20-30 A) water-in-oil microemulsion droplets (colloids) and large (radius 130-580 angstrom) nonadsorbing polymer chains have been investigated. Accepted theoretical scaling relations for describing correlations have been applied and do not account fully for the observations; solvency effects may account for the deviations. The polymer/colloid size ratio has been varied from around 4 to 19 by using three different molecular weights of polyisoprene. Small-angle neutron scattering (SANS) has been used to determine partial structure factors (PSF) through contrast variation. The structure factors describing colloid-colloid interactions for the three polymers at fixed polymer concentration are shown to exhibit the same scaling behavior as the phase boundaries, provided that samples are sufficiently far from the demixing phase transition. The structure factors show a dramatic increase at low wavevectors on approaching the phase boundary, and behavior in this region does not obey expected scaling relations. By calculating effective polymer Flory-Huggins parameters, the effect of apparent solvent properties on adding microemulsion are shown to be less dramatic for the higher molecular weight polymers. This study extends previous work carried out on microemulsion-polymer mixtures (Langmuir 2008, 24, 3053-3060).