Proteins are notoriously unstable. This causes protein drugs to be discarded and wasted and is inconvenient to patients. In addition it increases shipping and storage costs for the many scientists who use proteins in their research. We created two classes of polymers that are very effective stabilizers of proteins. The first class of polymers has trehalose in their side chains. The polymers can be either attached to the protein or simply added to stabilize the biomolecules to near boiling temperatures and repeated lyophilization. The polymers significantly outperform the native sugar, trehalose as well as other gold standards in the field like poly(ethylene glycol) (PEG). The second class of materials mimic the polysaccharide heparin and stabilize a growth factor important in wound healing, basic fibroblast growth factor (bFGF). We found that by conjugating the polymer to bFGF, the protein was rendered stable to a wide range of environmentally and therapeutically relevant stressors that normally inactivate it. For example, the protein is completely inactive when stored in the refrigerator, heated, subjected to enzymes, or exposed to weak or strong acid. Yet the bFGF-heparin mimicking polymer conjugate was stable to all of these stresses. These two polymer classes and their application will be discussed.