The chaperone-like activity of thermoresponsive polymers based on poly(dimethylaminoethyl methacrylate) (PDMAEMA) was studied on two different proteins, glyceraldehyde-3-phosphate dehydrogenase and chicken egg lysozyme. The polymers do not interact with the folded protein at room temperature but form a complex upon heating to either protein unfolding or polycation phase transition temperature. A PDMAEMA-PEO block copolymer with a dodecyl end-group (d-PDMAEMA-PEO) as well as PDMAEMA-PEO without the dodecyl groups protected the denatured protein against aggregation in contrast to PDMAEMA homopolymer. No effect of the polymers on the enzymatic activity of the client protein was observed at room temperature. The polymers also partially protected the enzyme against inactivation at high temperature. The results provide a platform for creation of artificial chaperones with unfolded protein recognition which is a major feature of natural chaperones. The thermoresponsive polymers can be also used for reversible sedimentation of the folded enzyme.