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In soft matter small angle neutron scattering (SANS) studies at large Q values, incoherent scattering becomes the dominant signal. In the Q-range of interest to this work, from 0.2 Å−1 to about 1.0 Å−1, the coherent scattering from the typical protein or polymer in a D2O buffer solution inevitably drops one to two orders of magnitude or more below the total scattering. Even after careful and accurate subtraction of the measured D2O buffer scattering, the remaining corrected, i.e. sample-only, signal will still be dominated by diffuse incoherent scattering from hydrogen in the sample itself. This is the exact region of interest when one wishes to probe the structural changes in “living” proteins caused by interactions and motions related to function. To further complicate the problem, there is strong motivation to measure this Q-regime at very low concentrations because it has been shown with wide angle X-ray scattering that proteins can undergo concentration-dependent structural changes that rapidly increase below concentrations of about 5% [1] motivating the study of protein solutions at ever lower concentrations. In this case the signal from the protein will inevitably become much less than the scattering of the D2O buffer solution it is contained in. Polarization analysis offers the opportunity to separate the weak coherent signal from the larger incoherent signal and perhaps enable measurements under the conditions described above. This paper will address the issues associated with the correct separation of coherent and incoherent scattering for soft matter samples. We have performed tests measurements on KWS2 which show the viability of the method on a protonated α-lactalbumin solution at 2.5% (1mm thick) and 0.25% (2mm thick) concentrations in a D2O buffer solution. Additionally describe a the method of implementation using 3He spin filters, some practical considerations, and future plans for a dedicated device at the JCNS. [ABSTRACT FROM AUTHOR]