Abstract
A new molecular thermodynamic description of the interactions of globular proteins and flexible nonionic polymers, which influence the partition of proteins in two-phase aqueous polymer systems is presented. The changing nature of the polymer solution phase from one of identifiable polymer coils to one of an entangled web or net of polymers, with increasing polymer molecular weight is described. In addition to the novel physical pictures proposed for the interactions of polymers and proteins in two-phase aqeous polymer systems, descriptions are proposed for the free energy of interaction within each of the pictures and this quantity is related through a statistical thermodynamic framework to the experimentally measured protein partition coefficient
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