Protein-polymer conjugation can significantly affect many different aspects of protein behavior, ranging from their solution properties to their ability to form solution and bulk nanostructured materials. An underlying fundamental question is how the molecular design affects the shape of the conjugate and, consequently, its properties. This work measures the molecular configuration of model protein-polymer conjugates in dilute solution using small-angle neutron scattering (SANS) and uses quantitative model fitting to understand the shape of the molecules. Form factor measurements of four model bioconjugates of the red fluorescent protein mCherry and the polymers poly(N-isopropylacrylamide), poly(hydroxypropyl acrylate), poly(oligoethylene glycol acrylate), and poly(ethylene glycol) show that these protein-polymer conjugates are well described by a recently developed scattering function for colloid-polymer conjugates that explicitly incorporates excluded volume interactions in the polymer configuration. In the regime where the protein does not exhibit strong interactions with the polymer, modeling the protein-polymer interactions using a purely repulsive Weeks-Chandler-Andersen potential also leads to a coarse-grained depiction of the conjugate that agrees well with its scattering behavior. The coarse-grained model can additionally be used for systems with varying protein-polymer interactions, ranging from purely repulsive to strongly attractive, which may be useful for conjugates with strong electrostatic or hydrophobic attractive interactions. (C) 2015 Wiley Periodicals, Inc.